BIOCHEMISTRY INVOLVED IN THE HOMEOPATHIC PRINCIPLE “SIMILIA SIMILIBUS CURENTUR”

SIMILIA SIMILIBUS CURENTUR is considered to be the most fundamental theory of homeopathy. It is the basic theoretical foundation upon which the whole superstructure of this therapeutic system is built up. Even though homeopaths consider it as a “natural law” of therapeutics, critics of homeopathy never accept such a law or pattern really rexists in nature. They use to portray it as a “natural fallacy” of Hahnemann!

When attempting to establish homeopathy as a scientific medical system, it is essential that we should be capable of providing a scientifically plausible explanation for the biological mechanism of cure involved in SIMILIA SIMILIBUS CURENTUR, and prove it according scientific method.

Samuel hahnemann, great founder of Homeopathy, says that a substance can cure a disease, if the symptoms produced by that substance in healthy individuals are SIMILAR to the symptoms expressed by the person in disease condition.

Looking from a scientific perspective, similarity of symptoms indicate similarity of affected biomolecular pathways, similarity of Molecular inhibitions, similarity of target molecules, similarity of involved drug molecules and pathogenic molecules, and ultimately, similarity of their functional groups.

In order to be capable of explaining similia Similibus Curentur’ scientifically, first of all, we have to study carefully the phenomenon known as COMPETITIVE INHIBITIONS in modern biochemistry.

AS all of us know, competitive inhibition is the interruption of a biochemical pathway owing to one chemical substance inhibiting the effect of another by competing with it for binding or bonding with same targets, due to the SIMILARITY of their FUNCTIONAL GROUPS.

Several classes of competitive inhibition are especially important in biochemistry and medicine, such as the competitive form of enzyme inhibition, the competitive form of receptor antagonism, the competitive form of antimetabolite activity, the competitive form of poisoning etc.

In competitive inhibition of enzyme catalysis, binding of an inhibitor prevents binding of the natural target molecule of the enzyme, also known as the substrate. This is accomplished by blocking the binding site of the enzyme, also known as the active site, where the natural ligands or substrates are expected to bind with.

Competitive inhibition can be overcome by adding more substrate or natural ligands to the reaction, which increases the chances of the enzyme and substrate binding. This is is known as reversibility of competitive inhibitions.

Most competitive inhibitors function by binding reversibly to the active site of the enzyme. As a result, many sources state that this is the defining feature of competitive inhibitors.

In competitive inhibition, an inhibitor having FUNCTIONAL GROUP similar to the normal substrate or ligand binds to the enzyme, usually at the active site, and prevents the substrate from binding. At any given moment, the enzyme may be bound to the inhibitor, the substrate, or neither, but it cannot bind both at the same time.

During competitive inhibition, the inhibitor and substrate compete for the same active site. The active site is a region on an enzyme which a particular protein or substrate can bind to. The active site will only allow one of the two complexes to bind to the site therefore either allowing for a reaction to occur or yielding it. In a state of competitive inhibition, the inhibitor molecules resemble the substrate and therefore take its place, thereby binding to the active site of an enzyme.

Increasing the substrate concentration would diminish the “competition” and help the natural substrate to properly bind to the active site and allow a reaction to occur. When the substrate is of higher concentration than that of the competitive inhibitor, it is more likely that the substrate will come into contact with the enzyme’s active site than the inhibitor.

Methotrexate is a chemotherapy drug that acts as a competitive inhibitor. It is structurally SIMILAR to the coenzyme called FOLATE, which binds to the enzyme dihydrofolate reductase. This enzyme is part of the synthesis of DNA and RNA, and when methotrexate binds the enzyme, it renders it inactive, so that it cannot synthesize DNA and RNA. Thus, the cancer cells are unable to grow and divide.

Another example of competitive inhibition involves prostaglandins which are made in large amounts as a response to pain, and can cause inflammatory process. Essential fatty acids form the prostaglandins, and when this was discovered, it turned out that these essential fatty acids are actually very good inhibitors to prostaglandins. These fatty acids inhibitors have been used as drugs to relieve pain because they can MIMIC as the substrate, and bind to the enzyme, and block prostaglandins due to their SIMILAR functional groups.

An example of non-drug related competitive inhibition is in the prevention of browning of fruits and vegetables. For example, tyrosinase, an enzyme within mushrooms, normally binds to the substrate, monophenols, and forms brown o-quinones. Competitive substrates, such as certain substituted benzaldehydes for mushrooms, compete with the substrate lowering the amount of the monophenols that bind. These inhibitory compounds added to the produce keep it fresh for longer periods of time by decreasing the binding of the monophenols that cause browning. This allows for an increase in produce quality as well as shelf life of mushrooms.

Competitive form of enzyme inhibition, the competitive form of receptor antagonism, the competitive form of antimetabolite activity, and the competitive form of poisoning

Ethanol (C2H5OH) serves as a competitive inhibitor to methanol and ethylene glycol for the enzyme alcohol dehydrogenase in the liver when present in large amounts. For this reason, ethanol is sometimes used as a means to treat or prevent toxicity following accidental ingestion of these chemicals.

Strychnine acts as an allosteric inhibitor of the glycine receptor in the mammalian spinal cord and brain stem. Glycine is a major post-synaptic inhibitory neurotransmitter with a specific receptor site. Strychnine binds to an alternate site that reduces the affinity of the glycine receptor for glycine, resulting in convulsions due to lessened inhibition by the glycine

After an accidental ingestion of a contaminated opioid drug desmethylprodine, the neurotoxic effect of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) was discovered. MPTP is able to cross the blood brain barrier and enter acidic lysosomes. MPTP is biologically activated by MAO-B, an isozyme of monoamine oxidase (MAO) which is mainly concentrated in neurological disorders and diseases. Later, it was discovered that MPTP causes symptoms similar to that of Parkinson’s disease. Cells in the central nervous system (astrocytes) include MAO-B that oxidizes MPTP to 1-methyl-4-phenylpyridinium (MPP+), which is toxic. MPP+ eventually travels to the extracellular fluid by a dopamine transporter, which ultimately causes the Parkinson’s symptoms. However, competitive inhibition of the MAO-B enzyme or the dopamine transporter protects against the oxidation of MPTP to MPP+. A few compounds have been tested for their ability to inhibit oxidation of MPTP to MPP+ including methylene blue, 5-nitroindazole, norharman, 9-methylnorharman, and menadione. These demonstrated a reduction of neurotoxicity produced by MPTP.

sulfanilamide competitively binds to the enzyme in the dihydropteroate synthase (DHPS) active site by mimicking the substrate para-aminobenzoic acid (PABA). This prevents the substrate itself from binding which halts the production of folic acid, an essential nutrient. Bacteria must synthesize folic acid because they do not have a transporter for it. Without folic acid, bacteria cannot grow and divide. Therefore, because of sulfa drugs’ competitive inhibition, they are excellent antibacterial agents.

An example of competitive inhibition was demonstrated experimentally for the enzyme succinic dehydrogenase, which catalyzes the oxidation of succinate to fumarate in the Krebs cycle. Malonate is a competitive inhibitor of succinic dehydrogenase. The binding of succinic dehydrogenase to the substrate, succinate, is competitively inhibited. This happens because malonate’s chemistry is similar to succinate. Malonate’s ability to inhibit binding of the enzyme and substrate is based on the ratio of malonate to succinate. Malonate binds to the active site of succinic dehydrogenase so that succinate cannot. Thus, it inhibits the reaction.

Competitive inhibition can be reversible or irreversible. If it is reversible inhibition, then effects of the inhibitor can be overcome by increasing substrate concentration. If it is irreversible inhibition, the only way to overcome it is to produce more of the target, and typically degrade, or excrete the irreversibly inhibited target.

In virtually every case, competitive inhibitors bind in the same binding site or active site as the substrate, but same-site binding is not an essential requirement for competitive inhibitions to happen. A competitive inhibitor could bind to an allosteric site of the free enzyme and prevent substrate binding, as long as it does not bind to the allosteric site when the substrate is bound. For example, strychnine acts as an allosteric inhibitor of the glycine receptor in the mammalian spinal cord and brain stem. Glycine is a major post-synaptic inhibitory neurotransmitter with a specific receptor site. Strychnine binds to an alternate site that reduces the affinity of the glycine receptor for glycine, resulting in convulsions due to lessened inhibition by the glycine.

Actually, it is this phenomenon of COMPETITIVE INHIBITIONS that works behind SIMILIMUM concept of homeopathy.

It actually means, a molecular inhibition produced by a particular pathogenic molecule could be removed by utilizing a drug molecule having competitive relationship with it due to the SIMILARITY of FUNCTIONAL GROUPS.

If the FUNCTIONAL GROUPS of pathogenic molecules and drug molecules are SIMILAR, they can bind to similar molecular targets and produce SIMILAR symptoms. That is why homeopathy tries to identify SIMILARITY between pathogenic molecules and drug molecules by observing the SIMILARITY of SYMPTOMS they produce.

Through the principle of SIMILIA SIMILIBUS CURENTUR, hahnemann was actually trying to explain and utilize this phenomenon of COMPETITIVE INHIBITIONS for the purpose of developing his new therapeutic method.

When we try to remove pathological molecular inhibitions by using competitive inhibitors as done in ALLOPATHY, there is always a chance for developing new DRUG induced DISEASES due to their off target actions. This phenomenon underlies the dangerous side effects of most of the chemotherapeutic drugs. It means, when we use ‘molecular forms’ of SIMILIMUM or “competitive inhibitors” for treating a disease, it may lead to establishing new diseases that may be more harmful to the organism. Hahnemann also observed this possibility of drug induced diseases, and he tried to overcome this danger by using potentized forms of competitive inhibitors or SIMILIMUM.

In order to overcome this adverse effects of competitive inhibitors when used for therapeutic purpose, Samuel hahnemann developed the technology of drug Potentization. Homeopathic POTENTIZATION involves a process of preparing MOLECULAR IMPRINTS of drug molecules in water-ethyl alcohol medium using drug molecules as templates.

Molecular imprints are supra-molecular clusters formed in the imprinting medium, wherein the spacial conformations of template molecules remain engraved as nanocavities. Due to complementary conformations, these molecular imprints of competitive inhibitors can act as ARTIFICIAL BINDING POCKETS for the pathogenic molecules and deactivate them, thereby removing the pathological molecular inhibitions they had produced in biological molecules.

If SYMPTOMS produced in healthy persons by a DRUG substance taken in its MOLECULAR form are found to be SIMILAR to those expressed by an individual in a particular DISEASE condition, that drug substance if applied in MOLECULAR IMPRINTED form can cure the particular disease condition of that individual.

DISEASE symptoms and DRUG induced symptoms appear SIMILAR when disease-producing substance and drug substance contain SIMILAR chemical molecules with SIMILAR functional groups or moieties, which can bind to SIMILAR biological targets, produce SIMILAR molecular inhibitions that lead to SIMILAR errors in SIMILAR biochemical pathways in the living system.

SIMILAR chemical molecules can COMPETE each other in binding to the same molecular targets.

DISEASE molecules produce diseases by competitively binding with the biological targets by mimicking as the natural ligands due to their conformational SIMILARITY.

DRUG molecules having conformational SIMILARITY with DISEASE molecules can can displace them by COMPETITIVE relationship, and thereby remove the pathological inhibitions they have produced in the biological molecules.

Anybody who can think rationally and scientifically will understand that SIMILIA SIMILIBUS CURENTUR is a natural objective phenomenon. It is not that much unscientific or PSEUDOSCIENCE as our skeptic friends try to make it appear!

This natural phenomenon was observed and described by Dr Samuel Hahnemann as ‘Similia Similibus Curentur’, the fundamental principle of homeopathy.

If symptoms produced in healthy individuals by a drug substance appear SIMILAR to the symptoms expressed in a disease condition, it obviously means that the particular drug substance as well as the particular disease-causing substance contain some chemical molecules having SIMILAR functional groups or moieties, so that both of them were capable of binding to same biological targets in the organism, producing SIMILAR molecular errors that are expressed through SIMILAR trains of symptoms.

MOLECULAR IMPRINTS of SIMILAR chemical molecules can act as ARTIFICIAL BINDING AGENTS for similar chemical molecules, and deactivate them due to their mutually complementary conformations.

It is obvious that Samuel Hahnemann was observing this phenomenon of COMPETITIVE relationship between SUBSTANCES in producing SIMILAR SYMPTOMS by acting upon living organisms.

Due to the historical limitations of scientific knowledge available to him, hahnemann could not understand that two different substances produce SIMILAR SYMPTOMS, only if both substances contain chemical molecules having functional groups or moieties of SIMILAR conformations, by which they could bind to SIMILAR biological targets and produce SIMILAR molecular inhibitions, that lead to SIMILAR deviations in SIMILAR biological pathways.

Remember, hahnemann was working during a period when modern biochemistry has not even evolved. It is obvious why hahnemann could not explain the phenomenon he observed using the paradigms of modern biochemistry. But his extraordinary genius could foresee its implications in therapeutics.

When a homeopath searches for a SIMILIMUM for his patient by matching DISEASE symptoms and DRUG symptoms, he is actually searching for a drug substance that contains some chemical molecules that have conformations similar to those of the particular chemical molecules that caused the disease, so that the drug molecules and disease-causing molecules will have a COMPETITIVE relationship in binding to the biological molecules.

Since MOLECULAR IMPRINTS of drug molecules contained in potentized forms of drug substance can act as ARTIFICIAL BINDING SITES for the disease-causing molecules having competitive relationship due to the CONFORMATIONAL affinity in between them and remove the pathological molecular inhibitions, post-avogadro dilutions of SIMILIMUM drug could be used as a therapeutic agent as per the principle SIMILIA SIMILIBUS CURENTUR.

HOMEOPATHY or SIMILIA SIMILIBUS CURENTUR is a therapeutic approach based on identifying drug molecules that are conformationally SIMILAR and capable of COMPETING with the disease-causing molecules in binding to their biological targets, by observing the SIMILARITY of disease symptoms as well as the symptoms drug substances could produce by applying on healthy individuals, and deactivating the disease-causing molecules by binding them using the MOLECULAR IMPRINTS of the similar drug molecules.

Once we could convince the scientific community that ‘Similia Similibus Curentur’ is based on the natural phenomenon of ‘COMPETITIVE RELATIONSHIP’ between chemical molecules having SIMILAR conformations in binding to the biological molecules that is well explained in modern biochemistry, homeopathy will be inevitably recognised as SCIENTIFIC!

Author: Chandran Nambiar K C

I started practicing homeopathy in 1970, when I was 20 years old and studying for final year of BSc (Zoology) course. My interest in homeopathy happened very accidentally, through a constant relationship with a local practitioner who happened to be father of my classmate. I was a regular visitor in his clinic, where from I started reading BOERICKE MATERIA MEDICA and other homeopathic books, which helped me to cure myself my troublesome asthma that have been haunting me since my childhood days. I became a voracious reader of homeopathy. I was also deeply involved in studying marxism and dialectical materialism during my college days, which attracted me to political activities. MARXISM and HOMEOPATHY became two essential parts of my intellectual and practical life, which still continues so. Even though I joined DHMS course in a karnataka homeopathic college, I could not continue it due to my intense involvement in revolutionary political activities that resulted in jail life and a lot of criminal cases. Once that phase was over, I took a diploma in veterinary science and became a livestock inspector in animal husbandry department under govt of kerala. I have been continuing my study and practice of homeopathy all through these years. Since CCH act came into force only in 1976, and it contained provisions allowing existing practitioners to continue, my homeopathic practice went smoothly in parallel with my government job. In 1987, co-operating with some local homeopaths and social activists, I started Kannur District Homeopathic Hospital Sociey, which established a chain of hospitals and homeopathic clinics in different parts of Kannur district. After a few years I had to leave the society for some political reasons, and I established a 100 bedded well equipped homeopathic hospital in Taliparamba, employing a number of prominent homeopaths. That was ended up as a financial disaster for me due to many reasons, including my lack of skills as a money manager, and I was compelled to close down my dream project with in a short period. I lost huge money I invested, lost my reputation, and it pulled me into a debt trap. I learned a lot of valuabl lessons from this failure- about life, human psychology, relationships, and above all, about myself. I realized failure is the greatest teacher, if you are prepared learn from it. I learned how will power and determination to win will help us come back into life as a phoenix from our own ashes. I learned, one does not fail unless he stops fighting and accepts failure. My failure and the hardships that followed has moulded my personality in such a way that I can now withstand any disaster and fight back. I tell you, you will not know what life really is, unless you miserably fail at least once in your life. By this time, I left my government job also, and settled as a full time homeopathic practitioner. By this practice, I could repair my earlier financial losses, and establish well in life. It was during this period that I felt the need of developing a simple and user-friendly homeopathic software, that resulted in the evolution of SIMILIMUM, which was later upgraded into SIMILIMUM ULTRA. Similimum Ultra was well accepted by the profession, and it collected good revenues which continues even today. I stopped my practice a few years back , and concentrated in the study and research activities to evolve scientifically viable explanations to the so-called riddles of homeopathy. This unrelenting study resulted in MIT or Molecular Imprints Therapeutics, which provides a scientific and rational explanation for homeopathy. I started a homeopathic discussion group on facebook called HOMEOPATHY FOR TOTAL CURE, which has more than 35000 homeopaths as members. By this work on facebook, I could establish close relationship with many homeopaths around the world. It goes on. I could successfully convert facebook as my office and work place, from where I propagate my MIT ideas, co-ordinate my works for homeopathic community, and sell my Similimum Ultra Software. My years of hardwork in search of HOW HOMEOPATHY WORKS ultimately resulted in the publication of a book titled REDEFINING HOMEOPATHY (3000 pages, 3 volumes, hard bound, Rs 6000), in which I have compiled my articles regarding my scientific explanations of basic principles of homeopathy. These ideas are called MIT or MOLECULAR IMPRINTS THERAPEUTICS. MIT is now included in the syllabus of MD (HOM) course of prestigious DY PATIL DEEMED UNIVERSITY, PUNE, INDIA. Research department of SARADA KRISHNA HOMEOPATHIC COLLEGE, Kulashekharam, Tamilnadu, India, the only NAC accredited homeopathy college in India, has recently taken up certain reserch projects for proving the scientific explanations proposed by MIT. Based on MIT perspective of homeopathy, I had developed an MIT PROTOCOL for scientific homeopathy, and initiated a project for establishing a chain of MIT NETWORK CLINICS all over India, where MIT PROTOCOL will be practiced. More over, I have developed a whole range of 351 MIT FORMULATIONS, which are disease-specific combinations of post-avogadro diluted homeopathy drugs. NOW I AM IN 71st YEAR OF MY LIFE, AND STILL LOOKING FOR NEW HORRIZONS!

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