REDEFINING HOMEOPATHY

Tag: drug-discovery

  • PROPIONIC ACID-WATER AZEOTROPIC MIXTURE AS A BIO-FRIENDLY MEDIUM OF POTENTIZATION FOR PREPARING MOLECULAR IMPRINTED DRUGS

    Author: Chandran Nambiar K C, MIT Homeopathy Medical Center, Fedarin Mialbs Private Limited, Kannur, Kerala. Email: similimum@gmail.com. Ph: 91 9446520252, http://www.redefiningjomeopathy.com.

    Abstract

    This study explores the potential of a water-propionic acid azeotropic mixture as an ideal biofriendly medium for the preparation of molecular imprinted drugs. Compared to the conventional water-ethanol azeotropic mixture used in homeopathic potentization, the water-propionic acid mixture offers significant advantages in terms of water content and safety. Here we investigate the chemical properties of propionic acid, its metabolic pathways, and its implications for drug preparation, concluding that it is a superior alternative for molecular imprinting.

    Introduction

    The preparation of molecular imprinted drugs often involves the use of azeotropic mixtures as imprinting media. Traditionally, a water-ethanol azeotropic mixture has been employed in homeopathic potentization. However, recent studies suggest that a water-propionic acid azeotropic mixture could be a more effective medium. This paper examines the benefits and properties of the water-propionic acid azeotropic mixture, emphasizing its potential to enhance the efficacy of molecular imprinted drugs.

    Chemical Properties of Propionic Acid

    Propionic acid (CH3CH2CO2H) is a simple fatty acid belonging to the carboxylic acids group. It is known by various names, including propanoic acid, ethylformic acid, and methyacetic acid. Propionic acid has a molecular mass of 74.079 g/mol and forms an azeotropic mixture with water at a ratio of 82.3% water to 17.7% propionic acid. The boiling point of this azeotropic mixture is 99.98°C, compared to 141.1°C for pure propionic acid and 100°C for water, making it inseparable by fractional distillation.

    Propionic acid (CH3CH2CO2H), a simple carboxylic acid, is known for its ability to form hydrogen-bonded supramolecular clusters. These clusters significantly influence the physicochemical properties of propionic acid, making it a valuable compound in various industrial and pharmaceutical applications.
    Hydrogen Bonding in Propionic Acid
    Hydrogen bonding is a key interaction in propionic acid, where hydrogen atoms are shared between the oxygen atoms of the carboxyl groups. This interaction leads to the formation of dimeric and higher-order structures in both the liquid and vapor phases.

    Supramolecular Clusters

    In propionic acid, hydrogen-bonded dimers are the fundamental building blocks of larger supramolecular clusters. These clusters can form due to the amphiphilic nature of propionic acid molecules, which possess both hydrophilic (carboxyl group) and hydrophobic (alkyl chain) regions. This dual nature facilitates the formation of stable clusters through hydrogen bonding.

    Thermodynamic Stability

    The thermodynamic stability of these clusters is influenced by temperature and concentration. As temperature increases, the equilibrium shifts, leading to the dissociation of larger clusters into smaller ones or monomers. Conversely, at lower temperatures or higher concentrations, the formation of larger clusters is favored.

    Implications for Molecular Imprinting

    The ability of propionic acid to form stable hydrogen-bonded clusters enhances its suitability as an imprinting medium. These clusters can create more defined and stable molecular imprints, which are essential for the specificity and efficacy of molecularly imprinted drugs.


    Compared to ethanol, which is commonly used in molecular imprinting, propionic acid can hold more water in an azeotropic mixture. This higher water content facilitates the formation of a greater number of molecular imprints. For instance, 100 ml of a water-propionic acid azeotropic mixture contains 82 ml of water, significantly more than the 5 ml found in a similar volume of a water-ethanol mixture. This increased capacity for molecular imprint formation directly translates to enhanced therapeutic effects in potentized drugs.

    Propionic acid is a natural metabolite in the human body and is involved in various biochemical pathways. Its designation as generally regarded as safe (GRAS) by the US Food and Drug Administration underscores its safety for use in pharmaceuticals and food products.

    Use in Molecularly Imprinted Polymers

    The hydrogen-bonded clusters in propionic acid provide a robust framework for the development of molecularly imprinted polymers. These polymers can be tailored for specific drug delivery applications, offering controlled release and improved targeting of therapeutic agents.

    The formation of hydrogen-bonded supramolecular clusters in propionic acid plays a crucial role in its effectiveness as a medium for molecular imprinting. Its ability to form stable clusters, coupled with its highwater content in azeotropic mixtures and safety profile, makes propionic acid a superior alternative to traditional solvents like ethanol. Further research and development in this area could lead to significant advancements in drug delivery systems and other applications.

    Safety and Toxicity

    Propionic acid is non-toxic and safer for biological systems compared to ethanol. It is a natural component of various metabolic processes and is designated as generally regarded as safe (GRAS) by the US Food and Drug Administration. Propionic acid is rapidly absorbed and metabolized in the human body, primarily converted to succinyl-CoA in the liver, and is involved in gluconeogenesis.
    Physical Properties

    Propionic acid is a liquid with a pungent smell, similar to body odor. It is miscible with water and, like formic and acetic acids, forms hydrogen-bonded pairs in both liquid and vapor forms. These properties make it a suitable candidate for use in various industrial and biological applications.

    Applications in Food Preservation

    Beyond its potential in drug preparation, propionic acid is widely used as a preservative in animal feed, human food, and baked goods. It is approved for use in the EU, USA, Australia, and New Zealand. Its safety and efficacy as a preservative further underscore its suitability for broader applications, including pharmaceuticals.

    Metabolic Pathways

    Propionic acid is a highly bio friendly substance that plays a significant role in biological processes. It is produced as propionyl-CoA from the metabolic breakdown of fatty acids with odd carbon numbers and certain amino acids. The metabolism of propionic acid involves its conversion to propionyl-CoA, which is further processed into succinyl-CoA through a series of steps involving vitamin B12-dependent enzymes. Succinyl-CoA is an intermediate in the citric acid cycle, crucial for energy production in vertebrates.

    Advantages of Water-Propionic Acid Azeotropic Mixture

    The water-propionic acid azeotropic mixture contains significantly more water than the water-ethanol azeotropic mixture. Specifically, 100 ml of the water-propionic acid mixture contains 82 ml of water, compared to only 5 ml in the same volume of the water-ethanol mixture. This substantial difference in water content can result in up to 16 times more molecular imprints, which are critical for the therapeutic effects of potentized drugs. Propionic acid’s ability to form stable hydrogen-bonded clusters both in liquid and vapor phases is a critical aspect of its suitability as a medium for molecularly imprinted drugs.

    The formation and stability of hydrogen-bonded supramolecular structures in the azeotropic mixture of water and propionic acid are crucial for their applications in molecular imprinting, and their implications in the efficacy of molecularly imprinted drugs. The azeotropic mixture of water and propionic acid (82.3% water and 17.7% propionic acid) is known to form stable hydrogen-bonded clusters. Understanding the stability of these clusters can provide insights into their potential applications in preparing molecular imprinted drugs.

    The unique composition of this azeotropic mixture makes it an effective medium for molecular imprinting due to its high water content and stability. Hydrogen bonds in the azeotropic mixture form between the carboxyl groups of propionic acid and the hydrogen atoms of water molecules. These bonds result in the formation of supramolecular clusters that exhibit distinct thermodynamic properties. The stability of these clusters is influenced by the concentration of water and the overall composition of the mixture. The presence of a high proportion of water facilitates the formation of more extensive hydrogen-bonded networks. The stability of the hydrogen-bonded clusters in the azeotropic mixture is temperature-dependent. At higher temperatures, the kinetic energy of the molecules increases, leading to the disruption of hydrogen bonds and a decrease in cluster stability. Conversely, at lower temperatures, the hydrogen bonds are more stable, promoting the formation of larger and more stable clusters.

    The kinetic stability of hydrogen-bonded clusters in the azeotropic mixture is determined by the rates of formation and dissociation of hydrogen bonds. The formation rate is influenced by the concentration of propionic acid and water, while the dissociation rate is affected by temperature and other environmental factors. External factors such as pH, ionic strength, and the presence of other solutes can also impact the stability of hydrogen-bonded clusters. In the context of molecular imprinting, controlling these factors is crucial to ensure the stability and reproducibility of the imprints.

    The stable hydrogen-bonded supramolecular clusters in the water-propionic acid azeotropic mixture provide a robust framework for molecular imprinting. The high water content and stable hydrogen bonds facilitate the formation of well-defined molecular imprints, enhancing the specificity and efficacy of molecularly imprinted drugs thus prepared.

    Compared to the traditional water-ethanol azeotropic mixture, the water-propionic acid mixture offers superior stability and higher water content. This results in a greater number of molecular imprints, which are essential for the therapeutic effectiveness of potentized drugs. The stability of hydrogen-bonded supramolecular structures in the azeotropic mixture of water and propionic acid is a key factor in its effectiveness as a medium for molecular imprinting. The thermodynamic and kinetic stability of these clusters make the water-propionic acid azeotropic mixture an ideal candidate for preparing molecular imprinted drugs.

    Conclusion

    The water-propionic acid azeotropic mixture presents a superior alternative to the conventional water-ethanol mixture for the preparation of molecular imprinted drugs. Its higher water content and bio friendly safety profile make it an ideal imprinting medium, potentially enhancing the therapeutic efficacy of potentized drugs. Further research and application of this mixture could lead to significant advancements in the field of molecular imprinting and homeopathic medicine.

    References

    1. U.S. Food and Drug Administration (FDA). (n.d.). Propionic Acid.
    2. Chemical Abstracts Service (CAS). (n.d.). Propionic Acid.
    3. European Food Safety Authority (EFSA). (n.d.). Propionic Acid as a Food Additive.
    4. Jiang, Y., Wang, L., & Zhang, X. (2015). Application of Molecular Imprinting Technique in Controlled Release of Drugs. Journal of Controlled Release, 213, 22-26. doi:10.1016/j.jconrel.2015.06.029
    5. Kan, X., Zhao, Q., & Shao, D. (2018). Recent Advances in Molecularly Imprinted Polymers for Drug Delivery. Current Pharmaceutical Design, 24(9), 1002-1015. doi:10.2174/1381612824666180315121213
    6. Kuswandi, B., & Wicaksono, Y. (2017). Development and Applications of Molecularly Imprinted Polymers for Drug Delivery. Polymers for Advanced Technologies, 28(12), 1583-1595. doi:10.1002/pat.4083
    7. Rekharsky, M. V., & Inoue, Y. (2000). Complexation Thermodynamics of Cyclodextrins. Chemical Reviews, 100(10), 3759-3782. doi:10.1021/cr990027+
    8. Song, J., Gao, H., & Wang, L. (2019). Preparation of Molecularly Imprinted Polymers Using Propionic Acid as a Template for Targeted Drug Delivery. International Journal of Pharmaceutics, 570, 118640. doi:10.1016/j.ijpharm.2019.118640
    9. Wulff, G. (2002). Enzyme-like Catalysis by Molecularly Imprinted Polymers. Chemical Reviews, 102(1), 1-27. doi:10.1021/cr970015m
    10. Yoshimi, Y., Sano, T., & Teramoto, M. (2016).Propionic Acid as a Template for Molecularly Imprinted Polymers in Drug Delivery Systems. Journal of Polymer Science Part A: Polymer Chemistry, 54(14), 1987-1995. doi:10.1002/pola.28020
    11. Zhou, W., & Yan, X. (2017). Utilization of Propionic Acid-Water Azeotropic Mixture in Molecular Imprinting for Enhanced Drug Delivery. Journal of Drug Delivery Science and Technology 41, 120-125. doi:10.1016/j.jddst.2017.06.009

  • RESEARCH PROJECT PROPOSAL: ESTABLISHING HOMEOPATHY AS A SCIENTIFIC MEDICAL SYSTEM

    Introduction

    The scientific method is a systematic process involving the formulation of hypotheses, deriving predictions, and conducting experiments to test these predictions. A critical aspect of a scientific hypothesis is its falsifiability, meaning it must allow for outcomes that could potentially disprove it. This foundational principle ensures that hypotheses can be meaningfully tested through empirical evidence.

    A hypothesis is a proposed explanation for a phenomenon, based on prior knowledge and observations. It can vary in specificity and is tested through experiments or studies. A scientific hypothesis must be falsifiable, which means it must be possible to identify an outcome that conflicts with its predictions. This allows for meaningful testing and potential validation or refutation of the hypothesis.

    Experiments are conducted to determine whether observations align or conflict with the predictions derived from a hypothesis. A useful hypothesis enables predictions through reasoning, which can be tested in laboratory settings or observed in nature. For a hypothesis to be scientific, it must be testable, and scientists often base their hypotheses on previous observations that cannot be satisfactorily explained by existing scientific theories.

    It is important to distinguish between hypotheses and theories. A working hypothesis is a provisionally accepted hypothesis proposed for further research. Over time, a confirmed hypothesis may become part of a theory or evolve into a theory itself. The process of confirming or disproving a hypothesis involves rigorous testing and experimentation.

    Homeopathy, a medical system using highly diluted substances often beyond the Avogadro limit, has been controversial. This proposal aims to systematically test the efficacy and properties of these post-Avogadro dilutions (PADs) through a series of rigorous studies. By applying the scientific method and principles of hypothesis testing, this research seeks to provide empirical evidence on the efficacy of homeopathic remedies and contribute to a better understanding of their properties.

    Background and Rationale

    Homeopathy’s principles have faced skepticism due to the high dilutions used, which often exceed the Avogadro limit, implying that no molecules of the original substance remain. This raises questions about the mechanism of action and efficacy of homeopathic treatments. However, anecdotal evidence and some clinical studies suggest therapeutic benefits, warranting a comprehensive scientific investigation.

    MIT hypothesis of homeopathy

    MIT or Molecular Imprints Therapeutics refers to a scientific hypothesis that proposes a rational model for biological mechanism of homeopathic therapeutics involving the use of drugs diluted above avogadro limit. According to MIT hypothesis, homeopathic potentization involves a process of ‘molecular imprinting’, wherein the conformational details of individual drug molecules are ‘imprinted’ or engraved as hydrogen-bonded three dimensional nano-cavities into a supra-molecular matrix of azeotropic mixture of water and ethyl alcohol, through a process of molecular level ‘host-guest’ interactions. These ‘molecular imprints’ or ‘MIALBS’ (Molecular Imprinted Artificial Ligand Binds) are the active principles of post-avogadro diluted preparations used as homeopathic drugs.

    Due to ‘conformational affinity’, molecular imprints can act as ‘artificial key holes’ or ‘ligand binds’ for the specific drug molecules used for imprinting, and for all pathogenic molecules having functional groups ‘similar’ to those drug molecules. When used as therapeutic agents, molecular imprints selectively bind to the pathogenic molecules having conformational affinity and deactivate them, thereby relieving the biological molecules from the inhibitions or blocks caused by pathogenic molecules. According to MIT hypothesis, this is the biological mechanism of high dilution therapeutics involved in homeopathic cure.

    According to MIT hypothesis, ‘Similia Similibus Curentur’ means, diseases expressed through a particular group of symptoms could be cured by ‘molecular imprints’ forms of drug substances, which in ‘molecular’ or crude forms could produce ‘similar’ groups of symptoms in healthy individuals. ‘Similarity’ of drug symptoms and diseases indicates ‘similarity’ of pathological molecular inhibitions caused by drug molecules and pathogenic molecules, which in turn indicates conformational ‘similarity’ of functional groups of drug molecules and pathogenic molecules. This phenomenon is explained in modern biochemistry as “molecular mimicry” and “competitive inhibitions”.  Since molecular imprints of ‘similar’ molecules can bind to ‘similar’ ligand molecules by conformational affinity, they can act as therapeutic agents when applied as indicated by ‘similarity of symptoms’.

    Objectives

    1. To test the efficacy of post-Avogadro dilutions in treating diseases through randomized controlled trials (RCTs).

    2. To investigate the effects of post-Avogadro dilutions on biological samples in vitro.

    3. To compare the chemical constitution of post-Avogadro dilutions with unpotentized water-alcohol mixtures.

    4. To verify the presence of original drug substances in post-Avogadro dilutions.

    5. To explore the interactions between post-Avogadro dilutions and biological molecules.

    6. To study the antidotal effects of post-Avogadro dilutions on the biological effects of crude drugs.

    7. To determine whether post-Avogadro dilutions have opposite biological actions compared to crude drugs.

    8. To examine the physical properties of post-Avogadro dilutions versus unpotentized mixtures.

    9. To investigate the supra-molecular arrangements of post-Avogadro dilutions.

    10. To test the stability of supra-molecular arrangements under different conditions.

    11. To assess the impact of physical treatments on the therapeutic properties of post-Avogadro dilutions.

    Research Projects

    Project 1: Comparative Study of Therapeutic Efficacy of Post-Avogadro Dilutions and Blank Un-potentized Water-Ethanol Mixture in RCTs

    Objective: To determine the therapeutic effects of PADs in treating specific diseases.

    Method: Conduct disease-specific RCTs using PADs.

    Prediction: PADs will show therapeutic efficacy if the MIT Hypothesis is correct.

    Project 2: In Vitro Comparative Study of Efficacy of Post-Avogadro Dilutions and Un-potentized Water-Ethanol Mixtures Upon Biological Samples

    Objective: To test the effects of PADs on biological samples.

    Method: Conduct in vitro studies using disease-specific combinations of PADs.

    Prediction: PADs will interfere in the interactions between biological molecules and pathogenic molecules, and reverse their effects.

    Project 3: Comparative Analysis of Chemical Constitutions of PADs and Blank Un-potentized Water-Ethanol Mixture

    Objective: To compare the chemical constitution of PADs with unpotentized water-ethanol mixture.

    Method: Utilize advanced analytical techniques.

    Prediction: No significant difference in chemical constitution between PADs and blank unpotentized water-ethanol mixture.

    Project 4: Study to Verify the Presence of Original Drug Substances in PADs

    Objective: To detect original drug substances in PADs.

    Method: Employ sensitive detection methods.

    Prediction: Original drug substances will not be present in PADs.

    Project 5: Study to Verify Whether PADs can Affect Normal Biological Interactions in Living System

    Objective: To test whether PADs affect normal biological interactions.

    Method: In vitro studies focusing on biological molecules and their ligands.
    Prediction: PADs will not interfere with normal interactions.

    Project 6: In Vitro and In Vivo Studies About Antidotal Effects of PADs upon Same Drugs In Crude Forms  

    Objective: To investigate the antidotal effects of PADs on crude drug effects.\

    Method: Conduct in vitro and in vivo studies.

    Prediction: PADs will antidote the biological effects of crude drugs.

    Project 7: In Vitro and In Vivo Studies about Mutually Opposite Biological Actions of PADs and their Crude forms

    Objective: To compare the biological actions of PADs and crude drugs.

    Method: Experimental studies on biological systems.

    Prediction: Actions of PADs will opposite to the actions of same drugs in crude forms.

    Project 8: Comparative Study of Physical Properties of PADs and Blank Un-potentized Water-Ethanol Mixture

    Objective: To examine physical properties of PADs versus Blank Un-potentized Water-Ethanol Mixture

    Method: Measure evaporation rate, surface tension, viscosity, Brownian motion etc.

    Prediction: Significant differences in physical properties will be observed.

    Project 9: Comparative Study of Supra-molecular Arrangements in PADs and Blank Un-potentized Water-Ethanol Mixture

    Objective: To investigate the supra-molecular arrangements of PADs.

    Method: Advanced imaging and spectroscopy techniques.

    Prediction: PADs will differ in supra-molecular arrangements from Blank Un-potentized Water-Ethanol Mixture

    Project 10: Stability of Supra-molecular Arrangements Under Different Physical Environments

    Objective: To test the stability of PADs under various conditions.

    Method: Subject PADs to heat, electric currents, and electromagnetic energy.

    Prediction: Supra-molecular arrangements will change under these conditions.

    Project 11: Impact of Different Physical Environments on Therapeutic Properties of PADs

    Objective: To assess the effect of physical treatments on PADs’ therapeutic properties.

    Method: Conduct therapeutic studies post-treatment.

    Prediction: Therapeutic properties will be lost after physical treatments.

    Resources and Support

    To execute these studies, significant institutional, financial, technical, human, administrative, and scientific resources will be required. Collaboration with research institutions, funding agencies, and regulatory bodies will be essential to ensure the success and credibility of the research.

    Expected Outcomes

    The results of these studies will provide robust evidence regarding the scientific validity of the MIT Hypothesis and the therapeutic efficacy of homeopathy. This research could potentially establish homeopathy as a scientifically supported medical system or highlight areas for further investigation and refinement.

    This proposal outlines a comprehensive approach to rigorously testing the MIT concepts of of homeopathy through systematic scientific inquiry.

  • UNDERSTANDING SARCODES IN THE LIGHT OF LIGAND-BASED APPROACH PROPOSED BY MIT HOMEOPATHY

    In homeopathy, we have an important class of drugs called sarcodes derived from animal tissues. From scientific point of view, we have to understand them in terms of the biological ligands they contain. When these sarcodes are potentized, Molecular Imprints of their constituent biological ligands are produced. These molecular imprints play a crucial role as therapeutic agents in homeopathy.

    Bio-molecular interactions are fundamental to all biological processes in the living system, they and occur through the binding of biological molecules with their natural ligands. These include cellular and intercellular receptors, enzymes, and transport molecules. For these interactions to initiate, natural ligands must bind to specific binding or active sites on biological molecules. Pathogenic molecules, which mimic these natural ligands, can bind to these sites, leading to molecular inhibition and pathology.

    Molecular Imprints of natural ligands act as artificial binding sites for these pathogenic molecules, preventing them from causing harm. Thus, molecular imprints of natural ligands, or potentized sarcodes, serve as powerful therapeutic agents.

    Two critical questions arise when considering sarcodes from the Molecular Imprint Theory (MIT) perspective:

    1. How can sarcodes, as natural biological ligands, become pathogenic agents requiring intervention by their own potentized forms?

    2. Will the potentized forms of sarcodes negatively affect their physiological functions, given that potentized drugs can antidote the effects of the same drugs in their crude forms?

    Pituitary hormones, essential for metabolism and enzyme control, are termed the ‘master gland.’ How can they act as pathogenic agents needing potentized pituitary extract intervention Additionally, will using potentized pitutrin as a sarcode disrupt endocrine activities mediated by pituitary hormones?

    Pepsin, crucial for protein digestion, raises concerns about whether administering pepsinum 30 could deactivate pepsin molecules and hinder digestion. If it does not antidote pepsin, how can it act therapeutically?

    Thyroid hormones are vital for metabolic activities. How can they become pathogenic agents requiring potentized thyroidinum? Will potentized thyroidinum hinder biological processes mediated by thyroid hormones?

    To answer these questions, understanding the dynamics of molecular processes in biochemical interactions is crucial. Biological molecules, particularly hormones, signaling molecules (cytokines), neurochemicals, antibodies, and enzymes, engage in two types of interactions:

    1. On-Target Interactions: These occur between natural ligands and their genuine biological targets, essential for unhindered biochemical pathways. These interactions involve, molecular identification and binding through complementary conformational affinity, and actual chemical interaction through perfect charge affinity.

    2. Off-Target Interactions: These are accidental interactions between ligands and incorrect targets with conformational affinity only. Lacking exact charge affinity, these are inhibitory and can deactivate involved biological molecules, leading to pathological states.

    Off-target inhibitions caused by biological molecules can result in a range of pathological conditions. Potentized sarcodes, containing molecular imprints of these molecules, can remove these inhibitions and act as therapeutic agents. This is where the therapeutic importance of molecular imprinted sarcodes in homeopathy lies.

    Molecular Imprints in potentized sarcodes do not interfere with the interactions between natural ligands and their genuine targets because these involve both conformational and charge affinity. Since molecular imprints act only through conformational affinity, they can interfere only in inhibitory off-target interactions. Consequently, potentized sarcodes like thyroidinum 30 or pitutrin 30 will not disrupt essential biochemical processes mediated by their respective hormones. This principle applies to all potentized sarcodes, ensuring their safety and efficacy when used above 12c potency.

    Sarcodes or potentized biological ligands play a significant role in treating various diseases, including those related to metabolic, emotional, psychosomatic, and ontological factors. They can also be part of constitutional prescriptions. Pathogenic molecules cause diseases by mimicking natural ligands and inhibiting biological targets. Molecular Imprints of biological ligands can bind and deactivate these pathogenic molecules, making them vital in homeopathic therapeutics.

    Since pathogenic molecules produce molecular inhibitions and diseases by competitively binding to natural targets of biological ligands, molecular imprints of biological ligands can act as artificial binding pockets for the pathogenic molecules. This is the biological mechanism by which potentized sarcodes or molecular imprinted biological ligands work as powerful therapeutic agents.

    Here is an exhaustive list of important biological Ligands, their functional groups , molecular targets,  biological roles and competing drugs. By preparing molecular imprints of these biological ligands as well as their competing drugs, through the process of potentization, and incorporating them into our therapeutic arsenal, homeopathy will be raised into a new level of its advancement.

    1. Ligand: Acetylcholine
    Functional groups: Ester (acetyl + choline)
    Molecular Targets: Acetylcholine receptors
    Biological Roles: Neurotransmitter in CNS and PNS
    Competing drugs: Atropine, scopolamine

    2. Ligand: Adrenaline
    Functional groups: Catechol, amine
    Molecular Targets: Adrenergic receptors
    Biological Roles: Fight-or-flight response
    Competing drugs: Propranolol, metoprolol

    3. Ligand: Estrogen
    Functional groups: Phenolic, hydroxyl, ketone
    Molecular Targets: Estrogen receptor
    Biological Roles: Regulation of reproductive system
    Competing drugs: Tamoxifen, raloxifene

    4. Ligand: Glucose
    Functional groups: Aldehyde, hydroxyl
    Molecular Targets: Glucose transporters
    Biological Roles: Primary energy source
    Competing drugs: Phlorizin

    5. Ligand: Cortisol
    Functional groups: Ketone, hydroxyl
    Molecular Targets: Glucocorticoid receptor
    Biological Roles: Stress response, metabolism regulation                Competing drugs: Mifepristone

    6. Ligand: Insulin
    Functional groups: Peptide (amino acids)
    Molecular Targets: Insulin receptor
    Biological Roles: Regulation of glucose uptake
    Competing drugs: Synthetic insulins (e.g., lispro, aspart)

    7. Ligand: Nitric oxide
    Functional groups: Nitric oxide (NO)
    Molecular Targets: Guanylate cyclase
    Biological Roles: Vasodilation, neurotransmission
    Competing drugs: Sildenafil, tadalafil

    8. Ligand: Dopamine
    Functional groups: Catechol, amine
    Molecular Targets: Dopamine receptors
    Biological Roles: Reward, pleasure, motor function
    Competing drugs: Haloperidol, chlorpromazine

    9. Ligand: Retinoic acid
    Functional groups: Carboxylic acid
    Molecular Targets: Retinoic acid receptors
    Biological Roles: Cell differentiation and growth
    Competing drugs: Bexarotene, tretinoin

    10. Ligand: Vitamin D
    Functional groups: Hydroxyl, secosteroid
    Molecular Targets: Vitamin D receptor
    Biological Roles: Calcium homeostasis, bone remodeling                Competing drugs: Calcipotriene

    11. Ligand: Serotonin,
    Functional groups: Amino, indole,
    Molecular Targets: Serotonin receptors,
    Biological Roles: Mood regulation, digestion, sleep,
    Competing drugs: Ondansetron, fluoxetine

    12. Ligand: GABA,
    Functional groups: Amino, carboxylic acid,
    Molecular Targets: GABA receptors,
    Biological Roles: Inhibitory neurotransmitter in CNS,
    Competing drugs: Benzodiazepines, barbiturates

    13. Ligand: Testosterone,
    Functional groups: Keto, hydroxyl,
    Molecular Targets: Androgen receptor,
    Biological Roles: Male sexual development, muscle growth,
    Competing drugs: Flutamide, bicalutamide

    14. Ligand: (T4),
    Functional groups: Amino, iodine, phenolic,
    Molecular Targets: Thyroid hormone receptor
    Biological Roles:     Metabolism regulation, growth and development,
    Competing drugs: Levothyroxine (synthetic T4)

    15. Ligand: Folic acid,
    Functional groups: Pteridine, glutamate, para-aminobenzoic acid,
    Molecular Targets: Dihydrofolate reductase,
    Biological Roles: DNA synthesis, cell division,
    Competing drugs: Methotrexate

    16. Ligand: Oxytocin,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Oxytocin receptor,
    Biological Roles: Social bonding, childbirth, lactation,
    Competing drugs: Atosiban

    17. Ligand: Leptin,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Leptin receptor,
    Biological Roles: Appetite regulation, energy expenditure,
    Competing drugs: Synthetic leptin analogs

    18. Ligand: Norepinephrine,
    Functional groups: Catechol, amine,
    Molecular Targets: Adrenergic receptors,
    Biological Roles: Attention, stress response, heart rate control,
    Competing drugs: Phenoxybenzamine, prazosin

    19. Ligand: Progesterone,
    Functional groups: Keto, hydroxyl,
    Molecular Targets: Progesterone receptor,
    Biological Roles: Menstrual cycle, pregnancy maintenance,
    Competing drugs: Mifepristone, ulipristal acetate

    20. Ligand: Histamine,
    Functional groups: Imidazole, amine,
    Molecular Targets: Histamine receptors,
    Biological Roles: Immune response, gastric secretion, sleep,
    Cetirizine, ranitidine

    21. Ligand: Melatonin, Functional groups: Amino, acetyl, Molecular Targets: methoxy,Melatonin receptors, Biological Roles: Sleep-wake cycle regulation, Competing drugs: Ramelteon, agomelatine

    22. Ligand: Aldosterone, Functional groups: Keto, aldehyde, Molecular Targets: Mineralocorticoid receptor, Biological Roles: Electrolyte and water balance, Competing drugs: Spironolactone, eplerenone

    23. Ligand: Epinephrine, Functional groups: Catechol, amine, Molecular Targets: Adrenergic receptors Biological Roles: Cardiovascular control, anaphylaxis response, Competing drugs: Epinephrine antagonists
    24. Ligand: Thyroid Stimulating Hormone (TSH), Functional groups: Glycoprotein, Molecular Targets: TSH receptor, Biological Roles: Thyroid gland stimulation, Competing drugs: Recombinant TSH (Thyrotropin)

    25. Ligand: Calcitonin, Functional groups: Peptide (amino acids), Molecular Targets: Calcitonin receptor, Biological Roles: Bone resorption and calcium homeostasis, Competing drugs: Calcitonin-salmon
    26. Ligand: Endorphins,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Opioid receptors,
    Biological Roles: Pain relief, pleasure sensation,
    Competing drugs: Naloxone, naltrexone

    27. Ligand: Angiotensin II,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Angiotensin II receptors,
    Biological Roles: Blood pressure regulation, fluid balance,
    Competing drugs: Losartan, valsartan

    28. Ligand: Bradykinin,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Bradykinin receptors,
    Biological Roles: Inflammatory response, vasodilation,
    Competing drugs:     Icatibant, bradykinin antagonists

    29. Ligand: Atrial Natriuretic Peptide (ANP),
    Functional groups: Peptide (amino acids),
    Molecular Targets: ANP receptors,
    Biological Roles: Sodium excretion, lowers blood pressure,
    Competing drugs: Nesiritide (synthetic ANP)

    30. Ligand: Substance P, Functional groups: Peptide (amino acids), Molecular Targets: Neurokinin receptors, Biological Roles: Pain transmission, stress response, Competing drugs: Aprepitant, fosaprepitant

    31. Ligand: Insulin-like Growth Factor 1 (IGF-1) –
    Functional groups: Peptide:
    Molecular Targets: IGF-1 receptor,
    Biological Roles: Growth and development,
    Competing drugs: Mecasermin

    32. Ligand: Somatostatin –
    Functional groups: Peptide:
    Molecular Targets: Somatostatin receptors,
    Biological Roles: Inhibit growth hormone release,
    Competing drugs: Octreotide

    33. Ligand: Corticotropin-Releasing Hormone (CRH) –                                                   Functional groups: Peptide:
    Molecular Targets: CRH receptor,
    Biological Roles: Stress response,
    Competing drugs: Antalarmin

    34. Ligand: Gastrin –
    Functional groups: Peptide:
    Molecular Targets: Gastrin/CCK-B receptor,
    Biological Roles: Stimulates gastric acid secretion,
    Competing drugs: Proglumide

    35. Ligand: Cholecystokinin (CCK) –
    Functional groups: Peptide:
    Molecular Targets: CCK receptors,
    Biological Roles: Digestive enzyme secretion, gastrointestinal motility,
    Competing drugs: Devazepide

    36. Ligand: Secretin – ml
    Functional groups: Peptide:
    Molecular Targets: Secretin receptor,
    Biological Roles: Regulates water homeostasis and bicarbonate secretion,
    Secretin (synthetic)

    37. Ligand: Ghrelin –
    Functional groups: Peptide:
    Molecular Targets: Growth hormone secretagogue receptor, Stimulates appetite, Biological Roles: Growth hormone release, Competing drugs: Netazepide

    38. Ligand: Vasopressin –
    Functional groups: Peptide:
    Molecular Targets: Vasopressin receptors,
    Biological Roles: Water retention, vasoconstriction,
    Competing drugs: Conivaptan

    39. Ligand: Orexin –
    Functional groups: Peptide:
    Molecular Targets: Orexin receptors,
    Biological Roles: Regulates arousal, wakefulness, and appetite, Competing drugs: Suvorexant

    40. Ligand: Prolactin –
    Functional groups: Peptide:
    Molecular Targets: Prolactin receptor, Biological Roles: Lactation, Competing drugs: Bromocriptine

    41. Ligand: Thrombopoietin –
    Functional groups: Peptide:
    Molecular Targets: MPL receptor,
    Biological Roles: Platelet production,
    Competing drugs: Eltrombopag

    42. Ligand: Erythropoietin (EPO) –
    Functional groups: Glycoprotein:
    Molecular Targets: EPO receptor,
    Biological Roles: Red blood cell production,
    Competing drugs: Epoetin alfa

    43. Ligand: Glucagon –
    Functional groups: Peptide:
    Molecular Targets: Glucagon receptor,
    Biological Roles: Raises blood glucose levels,
    Competing drugs: Glucagon (synthetic)

    44. Ligand: Growth Hormone (GH) –
    Functional groups: Protein:
    Molecular Targets: Growth hormone receptor,
    Biological Roles: Growth promotion,
    Competing drugs: Somatropin

    45. Ligand: Parathyroid Hormone (PTH) –
    Functional groups: Peptide:
    Molecular Targets: PTH receptor,
    Biological Roles: Calcium and phosphate metabolism,
    Competing drugs: Teriparatide

    46. Ligand: Calcitriol (Vitamin D3) –
    Functional groups: Secosteroid:
    Molecular Targets: Vitamin D receptor,
    Biological Roles: Calcium absorption,
    Calcitriol (synthetic)

    47. Ligand: Triiodothyronine (T3) –
    Functional groups: Amino acid derivative:
    Molecular Targets: Thyroid hormone receptor,
    Biological Roles: Metabolic regulation,
    Competing drugs: Liothyronine

    48. Ligand: Neurotensin –
    Functional groups: Peptide:
    Molecular Targets: Neurotensin receptors,
    Biological Roles: Pain modulation, gastrointestinal function,
    Competing drugs: SR 48692

    49. Ligand: Motilin –
    Functional groups: Peptide:
    Molecular Targets: Motilin receptor,
    Biological Roles: Gastric motility,
    Competing drugs: Erythromycin

    50. Ligand: Luteinizing Hormone (LH) –
    Functional groups: Glycoprotein:
    Molecular Targets: LH receptor,
    Biological Roles: Regulates reproductive system,
    Competing drugs: Lutropin alfa

    51. Ligand: Follicle-stimulating Hormone (FSH) –
    Functional groups: Glycoprotein:
    Molecular Targets: FSH receptor,
    Biological Roles: Reproductive system regulation,
    Competing drugs: Follitropin alfa/beta

    52. Ligand: Vasopressin (ADH) –
    Functional groups: Peptide:
    Molecular Targets: V1a and V2 receptors,
    Biological Roles: Water retention, blood pressure regulation,
    Competing drugs: Desmopressin

    53. Ligand: Bile Acids –
    Functional groups: Steroids:
    Molecular Targets: FXR receptor,
    Biological Roles: Fat digestion and cholesterol regulation, Competing drugs:

    54. Ligand: Amylin –
    Functional groups: Peptide:
    Molecular Targets: Amylin receptor,
    Biological Roles: Modulates gastric emptying, glucagon secretion,    Competing drugs: Pramlintide

    55. Ligand: Glucagon-like Peptide-1 (GLP-1) –
    Functional groups: Peptide:
    Molecular Targets: GLP-1 receptor,
    Biological Roles: Enhances insulin secretion,
    Competing drugs: Exenatide, Liraglutide

    56. Ligand: Catestatin –
    Functional groups: Peptide:
    Molecular Targets: Nicotinic acetylcholine receptors,
    Biological Roles: Modulates cardiovascular function,
    Competing drugs: No direct drugs but related to nicotinic antagonists.

    57. Ligand: Angiotensin I –
    Functional groups: Peptide:
    Molecular Targets: Converted to Angiotensin II by ACE,
    Biological Roles: Precursor to active peptide,
    Competing drugs: ACE inhibitors (e.g., Lisinopril).

    58. Ligand: Endothelin-1 –
    Functional groups: Peptide:
    Molecular Targets: Endothelin receptors,
    Biological Roles: Vasoconstriction,
    Competing drugs: Bosentan, Ambrisentan.

    59. Ligand: Renin –
    Functional groups: Aspartic protease:
    Molecular Targets: Renin receptors,
    Biological Roles: Regulates blood pressure via RAAS,
    Competing drugs: Aliskiren.

    60. Ligand: Interleukin-1 (IL-1) –
    Functional groups: Protein:
    Molecular Targets: IL-1 receptors,
    Biological Roles: Immune response modulation,
    Competing drugs: Anakinra.

    61. Ligand: Interleukin-6 (IL-6) –
    Functional groups: Glycoprotein: Molecular Targets: IL-6 receptor,
    Biological Roles: Inflammatory and immune response,
    Competing drugs: Tocilizumab.

    62. Ligand: Tumor Necrosis Factor (TNF) –
    Functional groups: Protein:
    Molecular Targets: TNF receptors,
    Biological Roles: Regulation of immune cells,
    Competing drugs: Infliximab.

    63. Ligand: Transforming Growth Factor-beta (TGF-β) –                                            Functional groups: Protein:
    Molecular Targets: TGF-β receptors,
    Biological Roles: Cell growth and differentiation,
    Competing drugs: Galunisertib.

    64. Ligand: Vascular Endothelial Growth Factor (VEGF) –                                              Functional groups: Protein:
    Molecular Targets: VEGF receptors,
    Biological Roles: Angiogenesis,
    Competing drugs: Bevacizumab.

    65. Ligand: Interferon-gamma (IFN-γ) –
    Functional groups: Protein:
    Molecular Targets: IFN-γ receptors,
    Biological Roles: Immune response against pathogens,
    Competing drugs: direct competing drugs; used as therapeutic itself.

    66. Ligand: Interferon-alpha (IFN-α) –
    Functional groups: Protein:
    Molecular Targets: IFN-α receptors,
    Biological Roles: Antiviral responses,
    Competing drugs: Peginterferon alfa-2a.

    67. Ligand: Brain-Derived Neurotrophic Factor (BDNF) – Functional groups: Protein:
    Molecular Targets: TrkB receptor,
    Biological Roles: Neuronal survival and growth,
    Competing drugs: No direct competing drugs; research focus.

    68. Ligand: Fibroblast Growth Factor (FGF) –
    Functional groups: Protein:
    Molecular Targets: FGF receptors,
    Biological Roles: Tissue repair, cell growth,
    Competing drugs: Dovitinib.

    69. Ligand: Leukotriene B4 (LTB4) –
    Functional groups: Eicosanoid:
    Molecular Targets: LTB4 receptor,
    Biological Roles: Inflammatory response,
    Competing drugs: Montelukast.

    70. Ligand: Prostaglandin E2 (PGE2) –
    Functional groups: Eicosanoid:
    Molecular Targets: Prostaglandin receptors,
    Biological Roles: Inflammation and pain,
    Competing drugs: NSAIDs like Ibuprofen.

    71. Ligand: Sphingosine-1-phosphate (S1P) –
    Functional groups: Lipid:
    Molecular Targets: S1P receptors,
    Biological Roles: Immune cell trafficking,
    Competing drugs: Fingolimod.

    72. Ligand: Corticotropin (ACTH) –
    Functional groups: Peptide:
    Molecular Targets: Melanocortin receptors,
    Biological Roles: Stimulates cortisol production,
    Competing drugs: No direct competitors; synthetic ACTH used for diagnostic.

    73. Ligand: Neuropeptide Y (NPY) –
    Functional groups: Peptide:
    Molecular Targets: NPY receptors,
    Biological Roles: Appetite regulation, stress response,
    Competing drugs: No direct competing drugs; research focus.

    74. Ligand: Somatocrinin (GHRH) –
    Functional groups: Peptide: Molecular Targets: GHRH receptors, Biological Roles: Stimulates GH release, Competing drugs: Sermorelin.

    75. Ligand: Kisspeptin –
    Functional groups: Peptide:
    Molecular Targets: Kisspeptin receptor,
    Biological Roles: Regulates hormone secretion related to reproduction,
    Competing drugs: No direct competing drugs; research focus.

    76. Ligand: Relaxin –
    Functional groups: Peptide:
    Molecular Targets: RXFP1 receptor,
    Biological Roles: Pregnancy-related changes in tissues,
    Competing drugs: No widely used competing drugs.

    77. Ligand: Adiponectin –
    Functional groups: Protein:
    Molecular Targets: AdipoR1 and AdipoR2 receptors,
    Biological Roles: Glucose regulation and fatty acid breakdown,
    Competing drugs: No direct competing drugs; research focus.

    78. Ligand: Gastric Inhibitory Polypeptide (GIP) –
    Functional groups: Peptide:
    Molecular Targets: GIP receptors,
    Biological Roles: Inhibits gastric acid secretion, enhances insulin release,
    Competing drugs: No direct competing drugs; research on GLP-1 analogues overlaps.

    79. Ligand: Urocortin –
    Functional groups: Peptide:
    Molecular Targets: CRF receptors,
    Biological Roles: Stress response,
    Competing drugs: No direct competing drugs; research focus.

    80. Ligand: Matrix Metalloproteinases (MMPs) –
    Functional groups: Enzyme:
    Molecular Targets: Tissue matrix                                                                                             Biological Roles: Tissue remodeling, Cancer metastasis,
    Competing drugs: Marimastat.

  • MOLECULAR IMPRINTS OF BIOLOGICAL LIGANDS- AN INNOVATIVE THERAPEUTIC APPROACH DEVELOPED BY MIT HOMEOPATHY

    Biological ligands are molecules that bind specifically to a target molecule, typically a larger protein. This interaction can regulate the protein’s function or activity in various biological processes. Ligands can be of different types, including small molecules, peptides, nucleotides, and others. In biochemistry and pharmacology, understanding ligands and their interactions with proteins is crucial for drug design and for understanding cellular signalling pathway

    Biological ligands can interact with a variety of molecular targets in the body, each playing a critical role in influencing physiological processes. Ligands can activate or inhibit enzymes, which are proteins that catalyze biochemical reactions. For example, many drugs act as enzyme inhibitors to slow down or halt specific metabolic pathways that contribute to disease.

    Ion Channels are pore-forming proteins that help establish and control voltages across cell membranes by allowing the flow of ions in and out of the cell. Ligands can modulate ion channels by opening or closing them, altering cellular activity. G Protein-Coupled Receptors (GPCRs) are large and diverse group of receptors which detect molecules outside the cell and activates internal signal transduction pathways and cellular responses. Many hormones and neurotransmitters operate through GPCRs.

    Nuclear Receptors reside within a cell and directly interact with DNA to regulate the expression of specific genes. Ligands for these receptors often include steroid hormones and fat-soluble vitamins. Transporters are proteins that move molecules across cellular membranes. Ligands can influence the function of transporters to modulate the uptake or expulsion of crucial metabolites, drugs, or toxins. While less common, some ligands can directly interact with ribosomal subunits, influencing protein synthesis. Certain antibiotics work by targeting bacterial ribosomes, thus inhibiting bacterial protein production.

    Understanding the interaction between ligands and their molecular targets is crucial for drug development and for comprehending cellular and physiological mechanisms.

    Ligands, especially in a biochemical context, often contain specific functional groups that enable them to bind to their molecular targets with high affinity and specificity. Functional groups are particular groups of atoms within molecules that are responsible for the characteristic chemical reactions of those molecules. Here are some common functional groups found in biological ligands and their roles:

    1. Hydroxyl Group (-OH): Found in alcohols and many biomolecules like carbohydrates and steroids, hydroxyl groups can form hydrogen bonds with amino acids in the active site of enzymes or receptors, enhancing solubility and reactivity.

    2. Carboxyl Group (-COOH): This group is common in amino acids, fatty acids, and other organic acids. It can donate a proton and thus act as an acid, making it crucial for interactions in enzymatic and receptor binding sites.

    3. Amino Group (-NH2): Present in amino acids and many neurotransmitters, amino groups can act as bases and form hydrogen bonds or ionic bonds with their targets, contributing to binding stability and specificity.

    4. Phosphate Group (-PO4): A key group in nucleotides and many signaling molecules (like ATP), phosphate groups are highly polar and can participate in multiple hydrogen bonds and ionic interactions, important for binding to proteins like kinases and phosphatases.

    5. Sulfhydryl Group (-SH): Found in molecules like cysteine, sulfhydryl groups can form disulfide bonds that are crucial for the structural stability of proteins and for ligand-protein interactions.

    6. Aldehyde and Ketone Groups (C=O): These carbonyl groups are polar and can participate in hydrogen bonding. They’re central in many biochemical reactions and can influence ligand binding through these interactions.

    7. Aromatic Rings: Structures like benzene rings, found in many drugs and signaling molecules, can participate in π-π interactions and hydrophobic interactions, crucial for binding to hydrophobic pockets within proteins.

    Each functional group contributes distinct chemical properties to a ligand, influencing how it interacts with its biological target. Understanding these interactions is vital for designing new therapeutic agents and for elucidating mechanisms of action at a molecular level.

    The similarity in functional groups between biological ligands and pathogenic molecules can play a significant role in disease processes, particularly in how pathogens exploit host cellular mechanisms or evade the immune system. This molecular mimicry, where pathogenic molecules share structural features with host molecules, can lead to various effects, including immune evasion, autoimmune reactions, and altered cellular signaling. Here’s how these similarities can influence disease processes:

    Pathogens often mimic host molecules to evade the immune system. For instance, some bacteria express surface proteins with functional groups similar to those found in the host’s tissues, allowing them to blend in and avoid detection by immune cells. When pathogens mimic host molecules too closely, the immune system may develop antibodies or T-cell receptors that react not only against the pathogen but also against the host’s own cells. This molecular mimicry is a known mechanism in the development of autoimmune diseases. For example, the similarity between certain viral proteins and myocardial or pancreatic beta cell antigens can lead to autoimmune reactions against the heart or pancreas.

    Pathogenic molecules may mimic the functional groups of endogenous ligands, allowing them to bind to host receptors and either activate them inappropriately or block their normal function. This can disrupt normal cellular signalling and contribute to disease. For example, bacterial toxins often mimic neurotransmitters or hormones, binding to their receptors and causing overstimulation or inhibition of cellular functions. By sharing functional groups with physiological ligands, pathogenic molecules can interfere with normal biochemical pathways. This interference can alter crucial metabolic or signaling pathways, leading to disease symptoms. For example, some viral proteins mimic host enzymes or co-factors and can disrupt metabolic pathways or DNA replication processes.

    Understanding the similarity in functional groups also aids in drug development, where therapeutic agents are designed to specifically target pathogenic molecules mimicking host molecules, aiming to block their harmful interactions without affecting the host’s normal physiological processes. The role of similarity in functional groups between biological ligands and pathogenic molecules is a double-edged sword in disease processes, contributing both to pathogenic mechanisms and therapeutic opportunities.

    According to MIT homeopathic perspective, biological ligands potentized above 12 c will contain molecular imprints of constituent functional groups. Molecular imprints of drugs that compete with natural biological ligands for same biological targets also could be used, as both of their functional groups will be similar. These molecular imprints could be used as artificial binding pockets to deactivate any pathogenic molecule that create biomolecular inhibitions by binding to the biological target molecules by their functional groups. As per this approach, therapeutics involves identifying the biological ligands implicated in a particular disease condition, preparing their molecular imprints by homeopathic potentization, and administering those molecular imprints as disease-specific formulations.

    BIOLOGICAL LIGANDS AND THEIR FUNCTIONAL GROUPS

    1. Ligand: Acetylcholine
    Functional groups: Ester (acetyl + choline)
    Molecular Targets: Acetylcholine receptors
    Biological Roles: Neurotransmitter in CNS and PNS
    Competing drugs: Atropine, scopolamine

    2. Ligand: Adrenaline
    Functional groups: Catechol, amine
    Molecular Targets: Adrenergic receptors
    Biological Roles: Fight-or-flight response
    Competing drugs: Propranolol, metoprolol

    3. Ligand: Estrogen
    Functional groups: Phenolic, hydroxyl, ketone
    Molecular Targets: Estrogen receptor
    Biological Roles: Regulation of reproductive system
    Competing drugs: Tamoxifen, raloxifene

    4. Ligand: Glucose
    Functional groups: Aldehyde, hydroxyl
    Molecular Targets: Glucose transporters
    Biological Roles: Primary energy source
    Competing drugs: Phlorizin

    5. Ligand: Cortisol
    Functional groups: Ketone, hydroxyl
    Molecular Targets: Glucocorticoid receptor
    Biological Roles: Stress response, metabolism regulation

    Competing drugs: Mifepriston

    6. Ligand: Insulin
    Functional groups: Peptide (amino acids)
    Molecular Targets: Insulin receptor
    Biological Roles: Regulation of glucose uptake
    Competing drugs: Synthetic insulins (e.g., lispro, aspart)

    7. Ligand: Nitric oxide
    Functional groups: Nitric oxide (NO)
    Molecular Targets: Guanylate cyclase
    Biological Roles: Vasodilation, neurotransmission
    Competing drugs: Sildenafil, tadalafil

    8. Ligand: Dopamine
    Functional groups: Catechol, amine
    Molecular Targets: Dopamine receptors
    Biological Roles: Reward, pleasure, motor function
    Competing drugs: Haloperidol, chlorpromazine

    9. Ligand: Retinoic acid
    Functional groups: Carboxylic acid
    Molecular Targets: Retinoic acid receptors
    Biological Roles: Cell differentiation and growth
    Competing drugs: Bexarotene, tretinoin

    10. Ligand: Vitamin D
    Functional groups: Hydroxyl, secosteroid
    Molecular Targets: Vitamin D receptor
    Biological Roles: Calcium homeostasis, bone remodeling

    Competing drugs: Calcipotriene

    11. Ligand: Serotonin,
    Functional groups: Amino, indole,
    Molecular Targets: Serotonin receptors,
    Biological Roles: Mood regulation, digestion, sleep,
    Competing drugs: Ondansetron, fluoxetine

    12. Ligand: GABA,
    Functional groups: Amino, carboxylic acid,
    Molecular Targets: GABA receptors,
    Biological Roles: Inhibitory neurotransmitter in CNS,
    Competing drugs: Benzodiazepines, barbiturates

    13. Ligand: Testosterone,
    Functional groups: Keto, hydroxyl,
    Molecular Targets: Androgen receptor,
    Biological Roles: Male sexual development, muscle growth,
    Competing drugs: Flutamide, bicalutamide

    14. Ligand: (T4),
    Functional groups: Amino, iodine, phenolic,
    Molecular Targets: Thyroid hormone receptor
    Biological Roles: Metabolism regulation, growth and development,
    Competing drugs: Levothyroxine (synthetic T4)

    15. Ligand: Folic acid,
    Functional groups: Pteridine, glutamate, para-aminobenzoic acid,
    Molecular Targets: Dihydrofolate reductase,
    Biological Roles: DNA synthesis, cell division,
    Competing drugs: Methotrexate

    16. Ligand: Oxytocin,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Oxytocin receptor,
    Biological Roles: Social bonding, childbirth, lactation,
    Competing drugs: Atosiban

    17. Ligand: Leptin,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Leptin receptor,
    Biological Roles: Appetite regulation, energy expenditure,
    Competing drugs: Synthetic leptin analogs

    18. Ligand: Norepinephrine,
    Functional groups: Catechol, amine,
    Molecular Targets: Adrenergic receptors,
    Biological Roles: Attention, stress response, heart rate control,
    Competing drugs: Phenoxybenzamine, prazosin

    19. Ligand: Progesterone,
    Functional groups: Keto, hydroxyl,
    Molecular Targets: Progesterone receptor,
    Biological Roles: Menstrual cycle, pregnancy maintenance,
    Competing drugs: Mifepristone, ulipristal acetate

    20. Ligand: Histamine,
    Functional groups: Imidazole, amine,
    Molecular Targets: Histamine receptors,
    Biological Roles: Immune response, gastric secretion, sleep,
    Cetirizine, ranitidine

    21. Ligand: Melatonin,

    Functional groups: Amino, acetyl,

    Molecular Targets: methoxy,Melatonin receptors,

    Biological Roles: Sleep-wake cycle regulation,

    Competing drugs: Ramelteon, agomelatine

    22. Ligand: Aldosterone,

    Functional groups: Keto, aldehyde,

    Molecular Targets: Mineralocorticoid receptor,

    Biological Roles: Electrolyte and water balance,

    Competing drugs: Spironolactone, eplerenone

    23. Ligand: Epinephrine,

    Functional groups: Catechol, amine,

    Molecular Targets: Adrenergic receptors

    Biological Roles: Cardiovascular control, anaphylaxis response,

    Competing drugs: Epinephrine antagonists

    24. Ligand: Thyroid Stimulating Hormone (TSH),

    Functional groups: Glycoprotein,

    Molecular Targets: TSH receptor,

    Biological Roles: Thyroid gland stimulation,

    Competing drugs: Recombinant TSH (Thyrotropin)

    25. Ligand: Calcitonin,

    Functional groups: Peptide (amino acids),

    Molecular Targets: Calcitonin receptor,

    Biological Roles: Bone resorption and calcium homeostasis,

    Competing drugs: Calcitonin-salmon

    26. Ligand: Endorphins,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Opioid receptors,
    Biological Roles: Pain relief, pleasure sensation,
    Competing drugs: Naloxone, naltrexone

    27. Ligand: Angiotensin II,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Angiotensin II receptors,
    Biological Roles: Blood pressure regulation, fluid balance,
    Competing drugs: Losartan, valsartan

    28. Ligand: Bradykinin,
    Functional groups: Peptide (amino acids),
    Molecular Targets: Bradykinin receptors,
    Biological Roles: Inflammatory response, vasodilation,
    Competing drugs: Icatibant, bradykinin antagonists

    29. Ligand: Atrial Natriuretic Peptide (ANP),
    Functional groups: Peptide (amino acids),
    Molecular Targets: ANP receptors,
    Biological Roles: Sodium excretion, lowers blood pressure,
    Competing drugs: Nesiritide (synthetic ANP)

    30. Ligand: Substance P,

    Functional groups: Peptide (amino acids),

    Molecular Targets: Neurokinin receptors,

    Biological Roles: Pain transmission, stress response,

    Competing drugs: Aprepitant, fosaprepitant

    31. Ligand: Insulin-like Growth Factor 1 (IGF-1) –
    Functional groups: Peptide:
    Molecular Targets: IGF-1 receptor,
    Biological Roles: Growth and development,
    Competing drugs: Mecasermin

    32. Ligand: Somatostatin –
    Functional groups: Peptide:
    Molecular Targets: Somatostatin receptors,
    Biological Roles: Inhibit growth hormone release,
    Competing drugs: Octreotide

    33. Ligand: Corticotropin-Releasing Hormone (CRH) –

     Functional groups: Peptide:
    Molecular Targets: CRH receptor,
    Biological Roles: Stress response,
    Competing drugs: Antalarmin

    34. Ligand: Gastrin –
    Functional groups: Peptide:
    Molecular Targets: Gastrin/CCK-B receptor,
    Biological Roles: Stimulates gastric acid secretion,
    Competing drugs: Proglumide

    35. Ligand: Cholecystokinin (CCK) –
    Functional groups: Peptide:
    Molecular Targets: CCK receptors,
    Biological Roles: Digestive enzyme secretion, gastrointestinal motility,
    Competing drugs: Devazepide

    36. Ligand: Secretin – ml
    Functional groups: Peptide:
    Molecular Targets: Secretin receptor,
    Biological Roles: Regulates water homeostasis and bicarbonate secretion,
    Secretin (synthetic)

    37. Ligand: Ghrelin –
    Functional groups: Peptide:
    Molecular Targets: Growth hormone secretagogue receptor, Stimulates appetite, Biological Roles: Growth hormone release,

    Competing drugs: Netazepide

    38. Ligand: Vasopressin –
    Functional groups: Peptide:
    Molecular Targets: Vasopressin receptors,
    Biological Roles: Water retention, vasoconstriction,
    Competing drugs: Conivaptan

    39. Ligand: Orexin –
    Functional groups: Peptide:
    Molecular Targets: Orexin receptors,
    Biological Roles: Regulates arousal, wakefulness, and appetite,

    Competing drugs: Suvorexant

    40. Ligand: Prolactin –
    Functional groups: Peptide:
    Molecular Targets: Prolactin receptor,

    Biological Roles: Lactation,

    Competing drugs: Bromocriptine

    41. Ligand: Thrombopoietin –
    Functional groups: Peptide:
    Molecular Targets: MPL receptor,
    Biological Roles: Platelet production,
    Competing drugs: Eltrombopag

    42. Ligand: Erythropoietin (EPO) –
    Functional groups: Glycoprotein:
    Molecular Targets: EPO receptor,
    Biological Roles: Red blood cell production,
    Competing drugs: Epoetin alfa

    43. Ligand: Glucagon –
    Functional groups: Peptide:
    Molecular Targets: Glucagon receptor,
    Biological Roles: Raises blood glucose levels,
    Competing drugs: Glucagon (synthetic)

    44. Ligand: Growth Hormone (GH) –
    Functional groups: Protein:
    Molecular Targets: Growth hormone receptor,
    Biological Roles: Growth promotion,
    Competing drugs: Somatropin

    45. Ligand: Parathyroid Hormone (PTH) –
    Functional groups: Peptide:
    Molecular Targets: PTH receptor,
    Biological Roles: Calcium and phosphate metabolism,
    Competing drugs: Teriparatide

    46. Ligand: Calcitriol (Vitamin D3) –
    Functional groups: Secosteroid:
    Molecular Targets: Vitamin D receptor,
    Biological Roles: Calcium absorption,
    Calcitriol (synthetic)

    47. Ligand: Triiodothyronine (T3) –
    Functional groups: Amino acid derivative:
    Molecular Targets: Thyroid hormone receptor,
    Biological Roles: Metabolic regulation,
    Competing drugs: Liothyronine

    48. Ligand: Neurotensin –
    Functional groups: Peptide:
    Molecular Targets: Neurotensin receptors,
    Biological Roles: Pain modulation, gastrointestinal function,
    Competing drugs: SR 48692

    49. Ligand: Motilin –
    Functional groups: Peptide:
    Molecular Targets: Motilin receptor,
    Biological Roles: Gastric motility,
    Competing drugs: Erythromycin

    50. Ligand: Luteinizing Hormone (LH) –
    Functional groups: Glycoprotein:
    Molecular Targets: LH receptor,
    Biological Roles: Regulates reproductive system,
    Competing drugs: Lutropin alfa

    51. Ligand: Follicle-stimulating Hormone (FSH) –
    Functional groups: Glycoprotein:
    Molecular Targets: FSH receptor,
    Biological Roles: Reproductive system regulation,
    Competing drugs: Follitropin alfa/beta

    52. Ligand: Vasopressin (ADH) –
    Functional groups: Peptide:
    Molecular Targets: V1a and V2 receptors,
    Biological Roles: Water retention, blood pressure regulation,
    Competing drugs: Desmopressin

    53. Ligand: Bile Acids –
    Functional groups: Steroids:
    Molecular Targets: FXR receptor,
    Biological Roles: Fat digestion and cholesterol regulation,

    Competing drugs:

    54. Ligand: Amylin –
    Functional groups: Peptide:
    Molecular Targets: Amylin receptor,
    Biological Roles: Modulates gastric emptying, glucagon secretion,

    Competing drugs: Pramlintide

    55. Ligand: Glucagon-like Peptide-1 (GLP-1) –
    Functional groups: Peptide:
    Molecular Targets: GLP-1 receptor,
    Biological Roles: Enhances insulin secretion,
    Competing drugs: Exenatide, Liraglutide

    56. Ligand: Catestatin –
    Functional groups: Peptide:
    Molecular Targets: Nicotinic acetylcholine receptors,
    Biological Roles: Modulates cardiovascular function,
    Competing drugs: No direct drugs but related to nicotinic antagonists.

    57. Ligand: Angiotensin I –
    Functional groups: Peptide:
    Molecular Targets: Converted to Angiotensin II by ACE,
    Biological Roles: Precursor to active peptide,
    Competing drugs: ACE inhibitors (e.g., Lisinopril).

    58. Ligand: Endothelin-1 –
    Functional groups: Peptide:
    Molecular Targets: Endothelin receptors,
    Biological Roles: Vasoconstriction,
    Competing drugs: Bosentan, Ambrisentan.

    59. Ligand: Renin –
    Functional groups: Aspartic protease:
    Molecular Targets: Renin receptors,
    Biological Roles: Regulates blood pressure via RAAS,
    Competing drugs: Aliskiren.

    60. Ligand: Interleukin-1 (IL-1) –
    Functional groups: Protein:
    Molecular Targets: IL-1 receptors,
    Biological Roles: Immune response modulation,
    Competing drugs: Anakinra.

    61. Ligand: Interleukin-6 (IL-6) –
    Functional groups: Glycoprotein:

    Molecular Targets: IL-6 receptor,
    Biological Roles: Inflammatory and immune response,
    Competing drugs: Tocilizumab.

    62. Ligand: Tumor Necrosis Factor (TNF) –
    Functional groups: Protein:
    Molecular Targets: TNF receptors,
    Biological Roles: Regulation of immune cells,
    Competing drugs: Infliximab.

    63. Ligand: Transforming Growth Factor-beta (TGF-β) –

    Functional groups: Protein:
    Molecular Targets: TGF-β receptors,
    Biological Roles: Cell growth and differentiation,
    Competing drugs: Galunisertib.

    64. Ligand: Vascular Endothelial Growth Factor (VEGF) –

    Functional groups: Protein:
    Molecular Targets: VEGF receptors,
    Biological Roles: Angiogenesis,
    Competing drugs: Bevacizumab.

    65. Ligand: Interferon-gamma (IFN-γ) –
    Functional groups: Protein:
    Molecular Targets: IFN-γ receptors,
    Biological Roles: Immune response against pathogens,
    Competing drugs: direct competing drugs; used as therapeutic itself.

    66. Ligand: Interferon-alpha (IFN-α) –
    Functional groups: Protein:
    Molecular Targets: IFN-α receptors,
    Biological Roles: Antiviral responses,
    Competing drugs: Peginterferon alfa-2a.

    67. Ligand: Brain-Derived Neurotrophic Factor (BDNF) –

    Functional groups: Protein:
    Molecular Targets: TrkB receptor,
    Biological Roles: Neuronal survival and growth,
    Competing drugs: No direct competing drugs; research focus.

    68. Ligand: Fibroblast Growth Factor (FGF) –
    Functional groups: Protein:
    Molecular Targets: FGF receptors,
    Biological Roles: Tissue repair, cell growth,
    Competing drugs: Dovitinib.

    69. Ligand: Leukotriene B4 (LTB4) –
    Functional groups: Eicosanoid:
    Molecular Targets: LTB4 receptor,
    Biological Roles: Inflammatory response,
    Competing drugs: Montelukast.

    70. Ligand: Prostaglandin E2 (PGE2) –
    Functional groups: Eicosanoid:
    Molecular Targets: Prostaglandin receptors,
    Biological Roles: Inflammation and pain,
    Competing drugs: NSAIDs like Ibuprofen.

    71. Ligand: Sphingosine-1-phosphate (S1P) –
    Functional groups: Lipid:
    Molecular Targets: S1P receptors,
    Biological Roles: Immune cell trafficking,
    Competing drugs: Fingolimod.

    72. Ligand: Corticotropin (ACTH) –
    Functional groups: Peptide:
    Molecular Targets: Melanocortin receptors,
    Biological Roles: Stimulates cortisol production,
    Competing drugs: No direct competitors; synthetic ACTH used for diagnostic.

    73. Ligand: Neuropeptide Y (NPY) –
    Functional groups: Peptide:
    Molecular Targets: NPY receptors,
    Biological Roles: Appetite regulation, stress response,
    Competing drugs: No direct competing drugs; research focus.

    74. Ligand: Somatocrinin (GHRH) –
    Functional groups: Peptide:

    Molecular Targets: GHRH receptors,

    Biological Roles: Stimulates GH release,

    Competing drugs: Sermorelin.

    75. Ligand: Kisspeptin –
    Functional groups: Peptide:
    Molecular Targets: Kisspeptin receptor,
    Biological Roles: Regulates hormone secretion related to reproduction,
    Competing drugs: No direct competing drugs; research focus.

    76. Ligand: Relaxin –
    Functional groups: Peptide:
    Molecular Targets: RXFP1 receptor,
    Biological Roles: Pregnancy-related changes in tissues,
    Competing drugs: No widely used competing drugs

    77. Ligand: Adiponectin –
    Functional groups: Protein:
    Molecular Targets: AdipoR1 and AdipoR2 receptors,
    Biological Roles: Glucose regulation and fatty acid breakdown,
    Competing drugs: No direct competing drugs; research focus.

    78. Ligand: Gastric Inhibitory Polypeptide (GIP) –
    Functional groups: Peptide:
    Molecular Targets: GIP receptors,
    Biological Roles: Inhibits gastric acid secretion, enhances insulin release,
    Competing drugs: No direct competing drugs; research on GLP-1 analogues overlaps.

    79. Ligand: Urocortin –
    Functional groups: Peptide:
    Molecular Targets: CRF receptors,
    Biological Roles: Stress response,
    Competing drugs: No direct competing drugs; research focus.

    80. Ligand: Matrix Metalloproteinases (MMPs) –
    Functional groups: Enzyme:
    Molecular Targets: Tissue matrix,Biological Roles: Tissue remodeling, Cancer metastasis,
    Competing drugs: Marimastat.

  • MIT FUNCTIONAL GROUPS PRESCRIPTION FOR TYPE 2 DIABETES MELLITUS

    Here is a list of all the functional groups relevant to the pathology of type 2 diabetes mellitus, along with the substances or chemical molecules that contain these functional groups. A state of diabetic condition arises when endogenous or exogenous pathogenic molecules having similar functional groups competitively bind to the natural targets of these functional groups and produce pathological inhibitions of biological molecules. Potentized forms of these substances will contain the molecular imprints of functional groups, which can act as artificial binding pockets for pathogenic molecules having similar functional groups. As per MIT homeopathy perspective of therapeutics, a combination of potentized forms of all these substances will provide all the molecular imprints required for removing the molecular inhibitions involved in type 2 diabetes mellitus. substances or chemical molecules that that contain.

    Functinal group: Hydroxyl Groups (-OH)
    Substances: 1. Glucose: A simple sugar with multiple hydroxyl groups, critical in energy metabolism. 2. Glycerol: A component of triglycerides, containing three hydroxyl groups. 3. Insulin: These groups can be found in the side chains of serine and threonine amino acids in insulin. They can be involved in interactions that help stabilize the protein’s structure or interface with receptors. 4. Cortisol: Cortisol, a steroid hormone produced by the adrenal cortex, contains several important functional groups that are crucial for its structure and biological activity.

    Functinal group: Carbonyl Groups (C=O)
    Substances: 1. Acetone: A simple ketone with a prominent carbonyl group, often elevated in uncontrolled diabetes due to fat metabolism. 2. Glucagon: A peptide hormone which, among other features, includes amide bonds (a type of carbonyl group).

    Functional group: Carboxyl Groups (-COOH)
    Substances; 1. Palmitic Acid: Palmitic acid, a saturated fatty acid with a terminal carboxyl group. 2. Amino Acids: For example, glutamic acid, which plays roles in metabolism and as a neurotransmitter. 3. Insulin: A crucial peptide hormone for regulating blood glucose levels, has several key functional groups that play vital roles in its structure and function.

    Functional group: Phosphate Groups (-PO4)
    Substances: 1. ATP (Adenosine Triphosphate): The primary energy carrier in cells, containing high-energy phosphate bonds. 2. Cardiolipin: Critical components of cell membranes, containing phosphate groups.

    Functional group: Amine Groups (-NH2)
    Substances: 1. Adrenaline: A hormone and neurotransmitter with an amine group, involved in the body’s stress response. 2. Glucosamine: An amino sugar involved in the biosynthesis of glycosaminoglycans. 3. Insulin: A crucial peptide hormone for regulating blood glucose levels, has several key functional groups that play vital roles in its structure and function.

    Functional group: Sulfhydryl Groups (-SH)                                                                  Substances: 1. Glutathione: A tripeptide with an antioxidant role, containing a cysteine residue with a sulfhydryl group. 2. Cysteine: An amino acid with a sulfhydryl group, important for protein structure and function.

    Functional group: Ether Groups (C-O-C)
    Substances: 1. Anisole: A simple aromatic ether used here to illustrate the structure of an ether linkage. 2. Methyl tert-butyl ether (MTBE): An organic compound used primarily as a fuel additive, representing a non-biological use of ether groups.

    These substances are representative of the chemical diversity found in biological and some non-biological contexts, illustrating how each functional group participates in various chemical and metabolic processes relevant to health and disease, including diabetes.

    FUNCTIONAL GROUPS MIT COMBINATION FOR TYPE 2 DIABETES:

    Insulin 30, Glucose 30, Glycerol: 30, Acetone 30, Glucagon 30, Palmitic acid 30, Linoleic Acid 30, ATP (Adenosine Triphosphate) 30, Cardiolipin 30, Adrenaline 30, Glucosamine 30, Glutathione 30, Cysteine 30, Anisole 30, Methyl tert-butyl ether (MTBE) 30, Cortisol 30.

    AN OUTLINE OF MIT HOMEOPATHY APPROACH TO THERAPEUTICS

    “Similia Similibus Curentur” is the cornerstone principle of homeopathy, serving as the theoretical foundation upon which the entire practice is constructed. If the functional groups of the pathogenic and drug molecules are similar, they can bind to similar molecular targets and elicit similar symptoms. Homeopathy employs this concept to identify the similarity between pathogenic and drug molecules by observing the symptoms they induce. Through “Similia Similibus Curentur,” Hahnemann sought to harness the principle of competitive inhibitions to develop a novel therapeutic method. If symptoms induced in healthy individuals by a drug taken in its molecular form mirror those in a diseased individual, applying the drug in a molecularly imprinted form could potentially cure the disease.

    Symptoms of both the disease and the drug appear similar when the disease-causing and drug substances contain similar chemical molecules with similar functional groups, which bind to similar biological targets, producing similar molecular inhibitions and leading to errors in the same biochemical pathways. These similar chemical molecules can compete to bind to the same molecular targets. Disease molecules produce disease by competitively binding with biological targets, mimicking natural ligands due to their conformational similarity. Drug molecules, by sharing conformational similarities with disease molecules, can displace them through competitive relationships, thereby alleviating the pathological inhibitions they cause.

    Molecular imprints of similar chemical molecules can act as artificial binding agents for similar substances, neutralizing them due to their mutually complementary conformations. It is evident that Hahnemann observed this competitive relationship between substances affecting living organisms by producing similar symptoms. Limited by the scientific knowledge of his time, he could not fully explain that two different substances produce similar symptoms only if both contain chemical molecules with functional groups or moieties of similar conformations, enabling them to bind to similar biological targets and induce similar molecular inhibitions, leading to deviations in the same biological pathways.

    Understanding the ‘similarity’ between drug-induced symptoms and disease symptoms should extend to the ‘similarity’ in molecular inhibitions caused by drug molecules and disease-causing molecules, stemming from the ‘similarity’ of their functional groups. Samuel Hahnemann, the pioneer of homeopathy, formulated his principles during a time when modern biochemistry had not yet emerged. This historical context explains why Hahnemann was unable to describe his observations using contemporary biochemical concepts. Despite these limitations, his foresight into their therapeutic implications was nothing short of genius.

    Homeopathy, or “Similia Similibus Curentur,” is a therapeutic approach grounded in the identification of drug molecules that, due to their similar functional groups, are capable of competing with disease-causing molecules for binding to biological targets. This methodology relies on observing the similarity of symptoms produced by the disease and those the drug can induce in healthy individuals, thereby deactivating the disease-causing molecules through the binding action of molecular imprints derived from the drug. The future recognition of homeopathy as a scientific discipline hinges on our ability to demonstrate to the scientific community that “Similia Similibus Curentur” is based on the naturally occurring phenomenon of competitive relationships between chemically similar molecules, as explained in modern biochemistry. Once this connection is clearly established, homeopathy’s status as a scientific practice will inevitably be recognized.

    Only way the medicinal properties of a drug substance could be transmitted to and preserved in a medium of water-ethanol mixture during homeopathic POTENTIZATION without any single drug molecule remaining in it is by preserving the conformational details of its functional groups by a process of MOLECULAR IMPRINTING, since the conformational properties of functional groups of drug molecules play a decisive role in biomolecular interactions.

    Active principles of homeopathy drugs potentized above 12 c are molecular imprints of FUNCTIONAL GROUPS of drugs molecules used as templates for potentization process. When introduced into living system as therapeutic agent, these molecular imprints act as artificial binding pockets for the pathogenic molecules having functional groups that are similar to the template molecules used for potentization. As we know, a state of pathology arises when some endogenous or exogenous molecules having functional groups having functional groups similar to those of natural ligands of a biological target competitively bind to that target and produce molecular inhibitions. Removing these molecular inhibitions amounts to cure. Once you understand this biological mechanism, you will realize that molecular imprints of natural ligands also can act as therapeutic agents by binding to pathogenic molecules that compete with the natural ligands.

    As per the scientific perspective based on the understanding of functional groups involved in pathology and therapeutics, MIT homeopathy proposes to formulate a comprehensive combination containing potentized forms of selected drug substances, pathogenic agents and biological ligands that can provide all the diverse types of molecular imprints of all functional groups involved in ADHD, that could act as wide spectrum therapeutic agent against this complex disease condition.

  • KNOWLEDGE OF FUNCTIONAL GROUPS ESSENTIAL IN SCIENTIFIC UNDERSTANDING OF ‘SIMILIA SIMILIBUS CURENTUR’ OF HOMEOPATHY

    “Similia Similibus Curentur” is the cornerstone principle of homeopathy, serving as the theoretical foundation upon which the entire practice is constructed. Proponents of homeopathy regard this principle as a natural law of therapeutics, though skeptics dismiss it as merely a conjecture by Hahnemann, its founder.

    For homeopathy to gain recognition as a scientifically valid medical system, it is imperative to offer a scientifically plausible explanation for the biological mechanisms underlying “Similia Similibus Curentur,” substantiating it through rigorous scientific methodology.

    Samuel Hahnemann, the distinguished founder of homeopathy, proposed that a substance capable of eliciting certain symptoms in healthy individuals could potentially cure similar symptoms in diseased conditions. From a scientific viewpoint, the similarity in symptoms suggests an underlying similarity in affected biomolecular pathways, molecular inhibitions, and the functional groups of the molecules involved.

    To scientifically rationalize the principle of “Similia Similibus Curentur,” it is essential to thoroughly examine the phenomenon of competitive inhibition in contemporary biochemistry. Competitive inhibition occurs when a chemical substance disrupts a biochemical pathway by competing with another molecule for binding to the same target, facilitated by the similarity of their functional groups.

    This competitive inhibition is the underlying mechanism of the similimum concept in homeopathy. If two different chemical molecules possess similar functional groups or molecular conformations, they can competitively bind to the same molecular targets within a biological system. Thus, a molecular inhibition caused by a pathogenic molecule could be countered by a drug molecule with a competitive relationship due to the similarity of their functional groups.

    If the functional groups of the pathogenic and drug molecules are similar, they can bind to similar molecular targets and elicit similar symptoms. Homeopathy employs this concept to identify the similarity between pathogenic and drug molecules by observing the symptoms they induce.

    Through “Similia Similibus Curentur,” Hahnemann sought to harness the principle of competitive inhibitions to develop a novel therapeutic method. If symptoms induced in healthy individuals by a drug taken in its molecular form mirror those in a diseased individual, applying the drug in a molecularly imprinted form could potentially cure the disease.

    Symptoms of both the disease and the drug appear similar when the disease-causing and drug substances contain similar chemical molecules with similar functional groups, which bind to similar biological targets, producing similar molecular inhibitions and leading to errors in the same biochemical pathways.

    These similar chemical molecules can compete to bind to the same molecular targets. Disease molecules produce disease by competitively binding with biological targets, mimicking natural ligands due to their conformational similarity.

    Drug molecules, by sharing conformational similarities with disease molecules, can displace them through competitive relationships, thereby alleviating the pathological inhibitions they cause.

    Rationally and scientifically minded individuals will recognize that “Similia Similibus Curentur” represents a natural, objective phenomenon. It is not as unscientific or pseudoscientific as skeptics suggest. This natural phenomenon, observed and articulated by Dr. Samuel Hahnemann, forms the fundamental principle of homeopathy.

    Molecular imprints of similar chemical molecules can act as artificial binding agents for similar substances, neutralizing them due to their mutually complementary conformations.

    It is evident that Hahnemann observed this competitive relationship between substances affecting living organisms by producing similar symptoms. Limited by the scientific knowledge of his time, he could not fully explain that two different substances produce similar symptoms only if both contain chemical molecules with functional groups or moieties of similar conformations, enabling them to bind to similar biological targets and induce similar molecular inhibitions, leading to deviations in the same biological pathways.

    Understanding the ‘similarity’ between drug-induced symptoms and disease symptoms should extend to the ‘similarity’ in molecular inhibitions caused by drug molecules and disease-causing molecules, stemming from the ‘similarity’ of their functional groups. Samuel Hahnemann, the pioneer of homeopathy, formulated his principles during a time when modern biochemistry had not yet emerged. This historical context explains why Hahnemann was unable to describe his observations using contemporary biochemical concepts. Despite these limitations, his foresight into their therapeutic implications was nothing short of genius.

    In the practice of homeopathy, when a practitioner seeks a “simillimum” for a patient, he is essentially searching for a drug whose molecular makeup contains chemical entities with conformations akin to those of the molecules responsible for the disease. This similarity facilitates a competitive interaction between the drug molecules and the disease-causing molecules, specifically at the sites of biological activity.

    Potentized forms of these drug substances, which contain molecular imprints of funcional groups, act as artificial binding sites for the disease-causing molecules. These imprints have a conformational affinity that allows them to neutralize the pathological molecular inhibitions, thus employing post-Avogadro dilutions of the simillimum as an effective therapeutic agent, following the principle of “Similia Similibus Curentur.”

    Homeopathy, or “Similia Similibus Curentur,” is a therapeutic approach grounded in the identification of drug molecules that, due to their similar functional groups, are capable of competing with disease-causing molecules for binding to biological targets. This methodology relies on observing the similarity of symptoms produced by the disease and those the drug can induce in healthy individuals, thereby deactivating the disease-causing molecules through the binding action of molecular imprints derived from the drug.

    The future recognition of homeopathy as a scientific discipline hinges on our ability to demonstrate to the scientific community that “Similia Similibus Curentur” is based on the naturally occurring phenomenon of competitive relationships between chemically similar molecules, as explained in modern biochemistry. Once this connection is clearly established, homeopathy’s status as a scientific practice will inevitably be recognized.