‘Molecular Imprinting in Water’ For Target-Specific Drug Designing- Science Behind Homeopathic Potentization
‘Drug designing’ is an advanced branch of modern pharmaceutical chemistry, which is involved with the process of developing new medicinal substances appropriate to the specific biological targets in the organism. Such a ‘designer drug’ is most commonly a small organic molecule which can inhibit or activate the functioning of a target biomolecule such as a protein, thereby resulting in a therapeutic process in the organism. Essentially, ‘drug designing’ involves the development of small molecules that are complementary in ‘shape’ and ‘charge’ to the biomolecular target to which they interact and therefore will bind to it. Modern drug designing protocols utilize computer modeling techniques also. This type of modeling is known as ‘computer-aided drug design’. Actually, ‘drug design’ is involved with ‘ligand’ design. Prediction of binding affinity of molecules to be designed is the first step in a successful modeling technique. Many other properties such as bioavailability, metabolic half life, lack of side effects, also should be optimized before a designed ‘ligand’ can become a safe and efficacious drug. Most of these ‘other’ characteristics are often very difficult to optimize using presently available drug design techniques.
Selection of drug target is most important in “drug designing”. A drug target is typically a key molecule involved in a particular metabolic or signaling pathway that is specific to a disease condition or pathology, or to the infectivity or survival of a microbial pathogen. Most of the therapeutic inteventions aim to inhibit the functioning of the ‘pathologic’ pathway in the diseased state by causing a key molecule to stop functioning. Drug molecules may be designed that bind to the active region and inhibit this key molecule. Some other therapeutic interventions actually enhance the ‘normal’ biochemical pathway by promoting specific molecules in the ‘normal’ pathways that may have been affected in the diseased state. Main challenge in all ‘drug therapies’ including ‘designer drugs’ is that these drug molecules should not affect any other important “off-target” molecules or ‘antitargets’ that may be similar in appearance to the target molecule, since drug interactions with off-target molecules may lead to undesirable side effects.
Designer drugs are small organic molecules produced through chemical synthesis, but biopolymer-based drugs (also known as biologics) produced through biological processes are becoming increasingly more common in modern drug designing.
‘Ligand-based drug design’ and ‘structure-based drug design’ are two major technologies now utilized in drug designing technologies.
Ligand-based drug design is based on the knowledge of other molecules that can bind to the biological target of interest. These other molecules may be used to derive a ‘pharmacophore’ which defines the minimum necessary structural characteristics a molecule must possess in order to bind to the target. In other words, a model of the biological target may be built based on the knowledge of what binds to it and this model in turn may be used to design new molecular entities that interact with the target.
Structure-based drug design is based on the knowledge of the three dimensional structure of the biological target obtained through methods such as x-ray crystallography or NMR spectroscopy. Using the structure of the biological target, candidate drugs that are predicted to bind with high affinity and selectivity to the target may be designed using interactive graphics.
Main draw back of ‘designer drugs’ is that there is a chance for these drug molecules affecting “off-target” molecules or ‘antitargets’ having similarity to the target molecules. Such interactions with off-target molecules may lead to grave consequences. Optimizing of various factors such as bioavailability, metabolic half life, and lack of side effects are the real challenges facing “drug designing” technology.
Molecular Imprinting in Polymers:
‘Molecular imprinting in polymers’ is a fast grownig research area that may be interesting to people engaged in developing “drug designing” techniques. A lot of research is currently going on over this subject the world over. This technology involves the imprinting of synthetic polymer substances using enzymes or such macromolecules as ‘guest’molecules. As a result of imprinting, nano cavities with 3-d spacial configurations complementary to the ‘guest’ molecules will be created in the interaction surfaces of the polymers. These imprinted polymers, by virtue of the nanocavities they contain can be used to bind molecules with configurational similarity to ‘guest’ molecules. They are at present widely used in various laboratory assays as powerful adsorption surfaces. MIPs are also found to be of much practical use in various areas of science and technology .
Molecular imprinted polymers of today cannot be used as therapeutic agents, since they are totally foreign substances to the organism. More over, native enzymes can not degrade the polymers even if they can play a therapeutic role in the organism.
Molecular imprinting may become part of future drug designing techniques, only if the search for safer substances and methods for molecular imprinting happens to be successful.
Molecular Imprinted Proteins:
Biopolymer-based drugs (also known as biologics) produced through biological processes are becoming increasingly more common in modern drug designing. But the revolutionary concept of molecular imprinting in proteins is only in its emerging stage, which may have implications in drug designing techniques. It has already been acknowledged that the biological molecules presently classified as antibodies are nothing but native globulin proteins subjected to natural molecular imprinting process with foreign pathologic proteins acting as ‘guest’ molecules. Scientists have already realized the fact that the much discussed pathologic molecules known as ‘prions’ are nothing but disfigured protein molecules subjected to molecular imprinting. Protiens, being polymers with complex and flexible tertiary structures, are expected to be a very good medium for molecular imprinting. Different types of protein based substances, subjected to artificial molecular imprinting, may evolve in the future as effective therapeutic agents and laboratory reagents.
Apart from protein molecules, different types of biopolymers such as polysaccharides and nucleic acids also may be experimented as medium for molecular imprinting.
Native proteins extracted from the patients could be subjected to molecular imprinting with appropriate ligands or other pathologic molecules acting as ‘guest’ molecules and used as target oriented therapeutic agents. But the problem remains that such imprinted proteins can be used only in the individual whose proteins are used for imprinting. Otherwise it may result in grave anaphylactic reactions. Moreover these imprinted proteins may remain in the organism for very long periods, without undergoing degradation, and cause ever new pathological molecular blocks. Such issues have to be addressed properly.
Molecular Imprinting in Water:
Our protracted search for a safe and reliable universal medium for molecular imprinted drug designing finally takes us to the study of wonderful physico-chemical properties of the most abundant substance on earth called water. But the concept and technology of molecular imprinting in water still remains in very infantile stage. The author is of the opinion that with its strange polymer-like behaviours, capable of forming hydrogen-bonded supra-molecular structures, water can be the ideal candidate for molecular imprinted drug designing in future.
Though in a slighly lesser level, Ethyl Alcohol and Lactose are also capable of forming polymer-like supra-molecular formations through hydrogen bonding, and hence may be onsidered as candidates for molecular imprinting experiments. Possibilities of these substances in combination with water also have to be explored.
Water(H2O) is a wonderful substance with strange physico–chemical properties arising from its peculiar supra-molecular structure. Water is a solvent with higher polarity than similar liquids. H–O–H bond angle is 105 degrees. That means, water molecule is a dipole. Because of this peculiarity, water molecules can exist like a supra-molecular network through hydrogen bonding. A minimum number of five water molecules will be contained in this network. Such supra-molecular formations are called pentamers. Most of the wonderful properties of water arise from this peculiar capacity of hydrogen bonding and resultant supra-molecular formations. Water molecules (H2O) are symmetric (point group C2ν) with two mirror planes of symmetry and a 2-fold rotation axis. The hydrogen atoms may possess parallel or antiparallel nuclear spin. The water molecule consists of two light atoms (H) and a relatively heavy atom (O). The approximately 16-fold difference in mass gives rise to its ease of rotation and the significant relative movements of the hydrogen nuclei, which are in constant and significant relative movement.
Although not often perceived as such, water is a very reactive molecule available at a high concentration. This reactivity, however, is greatly moderated at ambient temperatures due to the extensive hydrogen bonding. Each water molecules possess a strongly nucleophilic oxygen atom that enables many of life‘s reactions, as well as ionizing to produce reactive hydrogen and hydroxide ions. Reduction of the hydrogen bonding at high temperatures or due to electromagnetic fields results in greater reactivity of the water molecules.
As liquid water is so common-place in our everyday lives, it is often regarded as a ‘typical’ liquid. In reality, water is most atypical as a liquid, behaving as a quite different material at low temperatures to that when it is hot. It has often been stated that life depends on these anomalous properties of water. In particular, the high cohesion between molecules gives it a high freezing and melting point, such that we and our planet are bathed in liquid water. The large heat capacity, high thermal conductivity and high water content in organisms contribute to thermal regulation and prevent local temperature fluctuations, thus allowing us to more easily control our body temperature. The high latent heat of evaporation gives resistance to dehydration and considerable evaporative cooling. Water is an excellent solvent due to its polarity, high dielectric constant and small size, particularly for polar and ionic compounds and salts. It has unique hydration properties towards biological macromolecules (particularly proteins and nucleic acids) that determine their three-dimensional structures, and hence their functions, in solution. Hydration of biological molecules results in formation of gels that can reversibly undergo the gel-sol phase transitions that underlie many cellular mechanisms. Water ionize and allows easy proton exchange between molecules, thus contributing to the richness of the ionic interactions in living organisms.
In reality, hydrogen bonding is a special type of dipole force. It is a force of attraction formed between partial electro negative atom which is part of another molecule. The reason for strength is the partial positive charge attained by hydrogen. Hydrogen is capable of establishing similar bonds with the atoms of nitrogen, fluorine and oxygen. That is to say that the basis of hydrogen bonding is the attraction between one hydrogen atom which is part of a molecule which is attached to oxygen or nitrogen and oxygen or nitrogen which remains part of another molecule. This force is less powerful than the co–valent bonds which keeps the atoms inside molecule bound together. But these less powerful bonds are responsible for the wonderful bio–chemical qualities of water.
In the ordinary liquid state, in spite of 80% of the electrons being concerned with bonding, the three atoms in water do not stay together, as the hydrogen atoms are constantly exchanging between water molecules due to protonation/deprotonation processes. Both acids and bases catalyze this exchange and even when at its slowest (at pH 7), the average time for the atoms in an H2O molecule to stay together is only about a millisecond. As this brief period is, however, much longer than the timescales encountered during investigations into water’s hydrogen bonding or hydration properties, water is usually treated as a permanent structure.
The presence of ethyl alcohol in water is considered to be a factor reducing the rate of protonation/deprotonation processes, thereby enhancing the stability of hydration shells.
Hydrogen bond strength can be affected by electromagnetic and magnetic effects.
Any factors, such as polarization, that reduces the hydrogen bond length, is expected to increase its covalency. There is still some dispute over the size of this covalency, however any covalency will increase the network stability relative to purely electrostatic effects. As hydrogen bond strength depends almost linearly on its length (shorter length giving stronger hydrogen bonding), it also depends almost linearly (outside extreme values) on the temperature and pressure .
Hydrogen bonded chains (that is, O-H····O-H····O) are cooperative; the breakage of the first bond is the hardest, then the next one is weakened, and so on. Thus unzipping may occur with complex macromolecules held together by hydrogen bonding, for example, nucleic acids. Such cooperativity is a fundamental property of liquid water where hydrogen bonds are up to 250% stronger than the single hydrogen bond in the dimer. A strong base at the end of a chain may strengthen the bonding further.
Water-Ethyl Alcohol Mixture :
At this stage we have to understand a few facts about Ethyl Alcohol(CH3- CH2 – OH ). The molecules of alcohol also have the dipole structure as water molecules. It is possible for them to establish mutual connection through hydrogen bonding. The molecular weight of alcohol molecul is 46. The molecular weight of water(H2O) is 18. That means that the number of water molecules contained in 18 gram of water and the number of alcohol molecules contained in 46 gram of ethyl alcohol are equal. When alcohol and water are thoroughly mixed alcohol molecules network with water molecules through hydration bonds, The mobility of water molecules is restricted by the bonds established with alcohol molecules. Hence, hydration shells formed in alcohol–water mixture are comparatively more stable. The count of alcohol molecules and the count of water molecules contained in their mixture in 73:27 ratio will be equal. (73% w/w. alcohol and 27% w/w water) This mixturei is known as (40 power spirit).
Ideal medium for molecular imprining is supposed to contains 87% w/w of alcohol and 13% w/w of water. In this ratio, the number of alcohol molecules will be about more than that of of water molecules. Such a ratio will be very suitable for the production of stable hydration shells. More over, the presence of ethyl alcohol in water is considered as a factor reducing the rate of protonation/deprotonation processes, thereby enhancing the stability of hydration shells
We know that water is a good solvent. Let us see what happens when some foreign molecules are made to dissolve in water. If a foreign(called ‘guest’) molecule, ion, or colloidal particle happens to enter the matrix of 3-dimensional dynamic network of water molecules, they are entrapped inside this network. Water molecules arrange themselves around the ‘guest’ molecule in a peculiar way by the formation of hydrogen bonding. These formations of water molecules around the ‘guest’ molecules is known as hydration shells. These hydration shells exist in a dynamic state, and are more or less unstable. The ‘guest’ molecules dissolved in water exist in a state of being entrapped inside these hydration shells. This phenomenon can be seen both in ionic solutions and colloidal solutions. Obviously, hydration shells assume an internal spacial arrangement exactly fitting to the 3-dimensional spacial configuration of the ‘guest’ molecule entrapped in them. If we could devise some technique to remove the entrapped ‘guest’ molecules from these hydration shells, without disturbing the hydrogen bonds between the constituent water molecules, these hydration shells can retain the molecular memory of the molecular configurations of the removed ‘guest’ molecules. This rarely studied phenomenon underlies the much debated controversial ‘molecular memory of water’. Actual mechanism and forces underlying this phenomenon have to be investigated minutely by physical scientists. Minute changes occuring in the electron clouds of atoms of water molecules during the formation of hydration shells may be one factor responsible for this phenomenon. It has been well proven that these hydration shells later show a peculiar capability to differentially recognize the original ‘guest’ molecules which were responsible for their formation. This may be due to the existence of some imprinted memory of those host molecules retained in the hydration shells. This imprinting of memory may be compared to formation of finger prints. As in the case of finger prints, configuration of these molecular imprints also will be a complementary negative of ‘guest’ molecules. These empty hydration shells, or supra-molecular formations of water subjected to molecular imprinting, may be called ‘hydrosomes’, which means, minute ‘cavities of water’.
Homeopathic process of potentization may be a crude method of preparing hydrosomes, imprinted with various drug molecules(‘guest’), for utilizing as therapeutic agents. It should be specially noted that the medium used for homeopathic potentisation is not pure water, but it is mixed with ethyl alcohol in a particular ratio. It may be inferred that the presence of camparatively heavy ethyl alcohol molecules in this mixture may be contributing to stabilize the hydrosomes, preventing their easy dissociation. The convergent forces of rotational movements to which the mixture is subjected as part of homeopathic potentization, may also be a contributing factor in stabilizing the empty hydration shells.
This peculiar 3-d configuration of ‘hydrosomes’ are destroyed only when the energy level of water molecules are disturbed by the effect of heat, electricity, magnetism and other electro magnetic radiations. As stated earlier the hydration shells formed in pure water are comparatively unstable. Here lies the importance of the fact that homeopathic potencies are made using alcohol- water mixture.
Information we recently receive from various research institutions, regarding the wonderful supra-molecular structures of various materials and their hitherto unknown peculiar properties, may greatly contribute in our efforts to devise a protocol for molecular imprinted drug designing using water. Studies on ‘water clusters’, ‘crystalline structure of water’, ‘shape memory property’, ‘molecular imprinting’, ‘nano technology’, ‘clathrate formations’ and other diverse phenomena are offering promising indications in this direction. We have to utilize all these new revealations in our scientific study regarding the possibility of developing a technology of drug designing by molecular imprinting in water.
We all know that water exists as ice crystals in its solid form. But it has been recently observed that water can exist even in its liquid form in crystals. In reality, water formed by melting of ice is in a state of liquid crystals. The lattice structure which is formed through hydration bonds is responsible for this phenomenon. Molecular imprinting in water is much interested in this area of research pertaining to this peculiar crystalline nature of water. It is believed that in the process of molecular imprinting of water using ‘guest’ molecules, this crystalline structure of water plays a crucial role. It is likely that more advanced studies about dynamics of crystallization of water may help us to evolve a perfect technology for molecular imprinting in water.
The studies about Clathrate Compounds or host-guest compounds in supra-molecular chemistry is an area in which we should have sincere interest. Clathrates are the molecular networks which are formed when gases dissolve in water under high pressure. They exist in a peculiar host–guest relationship. The studies about this phenomenon are still in their infancy. Clathrates have a crystalline nature, existing as molecular networks, formed by a process of water molecules arranging around the guest molecules. The studies about the dynamics of clathrate formation are also likely to help in evolving a perfect protocol for molecular imprinting in water. Even if the host molecules are removed from clathrates, the network of water molecules have been found to remain intact. More over, the existing clathrates can induce the formation of similar clathrates. It will be very useful to consider these above discoveries connecting them with the phenomenon of molecular imprinting.
A lot of studies has been so far published regarding shape memory materials. Several alloys having crystalline structure have been observed to possess shape memory property. Such materials are known as SMART materials. This phenomenon also has to be understood well while trying to evolve a molecular imprinting technique of drug designing.
It is in the phenomenon of ‘molecular memory of water’ itself that we naturally land on when we attempt to develop molecular imprinted drugs. We have already seen that the alcohol–water molecules contained in the medium used for imprinting arrange themselves around the ‘guest’ molecules, and form hydration shells. We should develop a way to systematically remove the ‘guest’ molecules entrapped in the hydration shells, so that empty hydration shells or ‘hydrosomes’ remain. These ‘hydrosomes’ will be imprinted with the three-dimensional ‘finger print’ of ‘guest’ molecules used for imprinting.
When molecular imprinted water is introduced into the organism by any route, is carried by the body fluids, and transported to different parts of body. When molecular imprints come in the vicinity of ligands or active groups of pathological foreign molecules having similarity to the original ‘guest’ molecules, these molecular imprints selectively bind to those pathological molecules. By this process, pathological foreign molecules are prevented from binding with biological molecules, thereby relieving the biological molecules from pathological molecular blocks. This can be described as some sort of ‘molecular scavenging’ or entrapping of pathological molecules, by ‘hydrosomes’ or “molecular imrints”.
Drugs designed through molecular imprinting in water will be the safest of all therapeutic agents so far used in the history medical science. Though there is a chance for these molecular imprints affecting “off-target” molecules or ‘antitargets’ having similarity to the target molecules, such interactions will be of very transient nature, since these molecular imprints will be easily degraded into constituent water-ethyl alcohol molecules. Such temporary interactions with off-target molecules may not lead to any dangerous consequences. Factors such as bioavailability, metabolic half life, and lack of side effects also will be obviously remain in favorable range.
Using various ligands and pathological molecules involved in each disease process as ‘guest’ molecules, we can develop most appropriate specifc designer drugs against almost any disease. Instead of original pathological molecules or ligands, drug molecules having configurational similarity to them also can be used as “guest” molecules in the molecular imprinting protocol. Homeopathic potentization utilizes this strategy, which is the real essence of “similia similibus curentur”. I hereby appeal to the government and scientific community to take up this task with urgent priority, so that a whole new range of safe and effective designer drugs could be developed though this novel process of molecular imprinting in water.
Two Important Scientific Studies That Validate the Possibility of Molecular Imprinting in Homeopathic Potentization
As per the scientific explanation of homeopathy proposed by MIT or Molecular Imprints Therapeutics, potentized medicines contain MOLECULAR IMPRINTS or hydrogen bonded supra-molecular clusters of water/ethyl alcohol carrying the conformational imprints of drug molecules, which act artificial binding sites for pathogenic molecules and thereby removing the pathological molecular inhibitions.
One of the important predictions put forward to be verified for proving MIT was that supramolecular structure of potentized drugs will be different from that of unpotentized water-alcohol mixture, even though both contain same chemical molecules, which should be proved by tools and techniques of scientific methods.
I think the two remarkable works discussed below, one by Dr Tanmoy Maity, and the other by by Louis Rey, provide crucial support as very strong scientific proofs for this important prediction, thereby validating the MIT explanation of scientific homeopathy.
First study is one done by Tanmoy Maity (Department of Electrical Engineering, Indian School of Mines, Dhanbad, Jharkhand 826004, India), D. Ghosh & C.R. Mahata (Department of Electrical Engineering, Bengal Engineering and Science University, Shibpur, Howrah 711103, West Bengal, India), regarding effect of dielectric dispersion on potentised homeopathic medicines, which indicates a “rearrangement of vehicle molecules” in potentized drugs.
This report is available on
Second is one conducted by Louis Rey on thermo-luminescence of ultra-high dilutions of lithium chloride and sodium chloride, and published in December 2002, which is available in its full form at: http://www.janscholten.com/janscholten/Evidence_files/Rey.thermoluminescence.pdf E-mail address: firstname.lastname@example.org (L. Rey).
SCIENTIFIC EVIDENCE FOR RE-ARRANGEMENT OF VEHICLE MOLECULES DURING POTENTIATION :
This paper reports dielectric dispersion occurring in potentised homeopathic medicines subjected to variable frequency electric field using an instrumentation method developed by the authors. Oscillations occur in the direction of electric field, and are usually termed longitudinal/acoustic-mode vibrations.
The test material was lactose soaked with homeopathic medicine. Multiple resonance frequencies, forming a frequency-set, were observed repeatedly for each medicine.
The team reports experimental results for three potencies of Cuprum metallicum (Cuprum met) in the frequency range of 100 kHz–1 MHz. Each exhibits a set of resonance frequencies, which may be termed as its characteristic set. As the frequency-set of each medicine is different from those of others, each medicine may, therefore, be identified by its characteristic frequency-set. This suggests that potentised homeopathic medicines, which are chemically identical with the vehicle, differ from one another in the arrangement of vehicle molecules.
According to them, these “experiments show that potentised homeopathic medicines, which are chemically identical with the vehicle, differ from one another in the arrangement of vehicle molecules”.
“Difference in arrangement of vehicle molecules” strongly indicates the presence of “supra-molecular clusters of water and ethyl alcohol, into which the three-dimensional configuration of drug molecules are imprinted as nanocavities” as proposed by the hypothesis proposed by MIT.
The observation that “the resonance frequencies frequency-set of each medicine is different from those of others” strongly indicates clusters of water-ethyl alcohol molecules specifically rearranged in accordance with the shapes of constituent molecules of drug substance used for potentization.
Such a re-arrangement of vehicle molecules strongly indicates the process of ‘molecular imprinting’ happening during homeopathic potentization. Present work is a decisive step in the scientific understanding of homeopathy proposed by MIT.
SCIENTIFIC EVIDENCE FOR SUPRAMOLECULAR STRUCTURAL CHANGES IN POTENTIZING MEDIUM HAPPENING BY THE PROCESS OF POTENTIZATION:
As per the reported work, ultra-high dilutions of lithium chloride and sodium chloride (10−30g cm−3) have been irradiated by X- and gamma rays at 77 K, then progressively re-warmed to room temperature. During that phase, their thermo-luminance has been studied and it was found that, despite their dilution beyond the Avogadro number, the emitted light was specific of the original salts dissolved initially.
This wonderful observation that high dilutions of salts very much above avogadro number retains the specific thermo-luminance patterns reminding of of original salts seems to be very crucial. This phenomenon could be well explained only in terms of supramolecular nanostructures of water carrying the imprints of exact ‘conformations’ of ‘individual’ molecules of salts, as explained by MIT concepts.
Thermo-luminance studies have been developed and utilized so far as a “tool to study the structure of solids, mainly ordered crystals”. In the present study, the researchers successfully utilized it in ultra-high aqueous dilutions, which demonstrates the short range ‘crystalline’ character of water as well as high dilution preparations.
Actually, the researchers took up this work to ‘challenge’ the ‘water memory’ theory, but proved it otherwise. They confess in their report: “we thought that it would be of interest to challenge the theory according which preexistent ‘structures’ in the original liquid, developed around some added chemicals, could survive a great number of successive dilutions when done under vigorous mechanical stirring”.
Another important point to be noted is that the researchers did not use ‘commercial samples’ as most ‘researches’ do, but prepared themselves 15c dilutions of lithium chloride and sodium chloride under the guidance of boiron labs. This fact provides more scientific credence to this study.
The study “showed quite clearly that the initial addition of a solute (NaCl and LiCl) in the original D2O leaves a permanent effect even when, by successive dilutions made under strong vibration, all traces of solute have disappeared.” The results were reproduced in several repeated experiments, “beyond any ambiguity”.
Thermally stimulated luminance—often called thermo-luminance—is a well known phenomenon amongst the thermally stimulated processes (thermally stimulated conductivity—thermally stimulated electron emission—thermogravimetry—differential thermal analysis and differential scanning calorimetry, etc.). Its theory and applications have been fully developed inter alia by McKeever, Chen and Visocekas and it proved to be a most interesting tool to study the structure of solids, mainly ordered crystals. To that end, the studied material is “activated” at low-temperature, usually by radiant energy (UV, X-rays, gamma rays, electron beams, or neutrons) which most generally creates electrons–holes pairs which become separately “trapped” at different energy levels. Then, when the irradiated material is warmed up, the heating serves as a trigger to release the initially accumulated energy and the trapped electrons and holes move and recombine. A characteristic glow is emitted most often under the shape of different successive peaks according to the depths of the initial traps. As a general rule this phenomenon is observed in ordered crystals though it can be equally seen in disordered materials such as glasses. In that mechanism, imperfections in the lattice play a major role and are considered to be the place where luminance centres appear. Thus, thermoluminance is a good tool to study these imperfections and understand how they appear in the crystal.
This is exactly along those lines that the researchers carried our first investigations, starting, this time, from liquids which were turned into stable solids by low-temperature cooling.
Working essentially with water—mainly deuterium oxide—they have shown that the thermoluminance glow of irradiated hexagonal ice consisted in two major peak areas—Peak 1 near 120 K and Peak 2 near 166 K having well-defined emission spectra the D2O samples giving a much higher signal than the H2O ones.
In both cases, un-irradiated samples gave no signals whatsoever. For both D2O and H2O it was shown that the relative intensity of the thermoluminance glow was a function of the irradiation dose and, that at least for Peak 2, it did show a maximum between 1 and 10 kGy .
As a first hypothesis on the nature of the emission itself it has been suggested by Teixeira that Peak 2 could be connected to the hydrogen-bond network within the ice which, in turn, could result from the structure of the original liquid sample, whilst Peak 1 looked to be closely related to the molecule. This strengthens the views on the involvement of hydrogen bonds in this mechanism.
To develop this concept further, the researchers did select to study the effect of lithium chloride on the thermoluminescence of irradiated D2O ice since this particular substance is known to suppress hydrogen bonds. The result, indeed, is spectacular and, at the relatively low concentration of 0:1M, Peak 2 is totally erased whereas the basic emission of Peak 1 remains almost unchanged.
At that point the researchers thought that it would be of interest to challenge the theory according which pre-existent “structures” in the original liquid, developed around some added chemicals, could survive a great number of successive dilutions when done under vigorous mechanical stirring.
To that end they prepared, courtesy of the BOIRON LABORATORIES, ultra-high dilutions of lithium chloride and sodium chloride by successive dilutions to the hundredths, all done under vigorous mechanical stirring (initially 1 g in 100 cm3, then 1 cm3 of this solution in 99 cm3 of pure D2O … and so on) until they reached— theoretically—at the 15th dilution, a “concentration” of10−30 g cm−3. A reference sample of D2O alone was also prepared according to this technique, still keeping vigorous agitation (150 strokes=7:5 s at each successive “dilution” step).
They did proceed, then, to the “activation” of these materials by irradiation according the following experimental protocol.
One cubic centimeter of each solution is placed in aluminium test cavities of 20 mm diameter and 2 mm depth and frozen to −20◦C on a cold metallic block. The frozen systems are kept 24 h at −20◦C to achieve stability into their crystallization patternand they are immersed into liquid nitrogen and kept at −196◦C for 24 h.
In a first set of experiments the frozen ice disks are irradiated at 77 K with 100 kV X-rays to achieve a dose of 0:4 kGy (30 min). Previous determinations were done to check that the disks having identical positions in the field did receive the same dose (dosimetry has been done using Harwell, FWT, and alanine dosimeters).
After irradiation, all the “activated” samples are transferred into a liquid nitrogen container and kept, there, for a week-time, to even out whatever small differences could exist between them.
Finally, all samples are placed in the thermoluminance equipment and their respective glow recorded—with both a photo-multiplier and a CCD camera connected to a spectrograph—in the course of rewarming (3=min) between 77 and 13 K, as has been done in our previous published experiments.
Much to their surprise, the experimental results do show—without any ambiguity— that for an X-ray dose of 0:4 kGy the thermoluminescence glows of the three systems were substantially different. These findings did prove to be reproducible in the course of many different identical experiments.
To compare the curves between them the researchers normalized the emitted light readings taking Peak 1 as the reference. In doing so, we obtain for Peak 2 the different curves presented which show quite clearly that the initial addition of a solute (NaCl and LiCl) in the original D2O leaves a permanent effect even when, by successive dilutions made under strong vibration, all traces of solute have disappeared. More remarkable were the fact that, by far, lithium chloride demonstrates a stronger hydrogen bond suppressing “ghost” effect which could be related to the larger size of the lithium ion.
A second set of experiments done with gamma rays (courtesy of CELESTIN Reactor, COGEMA, Marcoule), at a higher dose (19 kGy) did confirm these findings
It appears, therefore, that the structural state of a solution made in D2O can be modified by the addition of selected solutes like LiCl and NaCl. This modification remains even when the initial molecules have disappeared and the effect is the same at different irradiation doses (0.4 –19 kGy) and for different radiant sources (X-rays, gamma rays). As a working hypothesis, the researchers propose that this phenomenon results from a marked structural change in the hydrogen bond network initiated at the onset by the presence of the dissolved ions and maintained in the course of the dilution process, probably thanks to the successive vigorous mechanical stirrings.
Researchers had no any idea of Molecular Imprinting. They proposes the following hypothesis for explaining their observation:
“As a working hypothesis, we propose that this phenomenon results from a marked structural change in the hydrogen bond network initiated at the onset by the presence of the dissolved ions and maintained in the course of the dilution process, probably thanks to the successive vigorous mechanical stirrings.”
See, this hypothesis comes very close to the concept of Molecular Imprinting!
If we fail to explain the observations of this monumental research in terms of Molecular Imprinting, there remains the danger that it will be hijacked by ‘energy medicine’ theoreticians, by interpreting in terms of ‘essence of drugs’, ‘information’, ‘vibrations’ and the like. Actually, Jan Scholten has already done such an exercise, by saying ‘information’ of drugs imprinted in water are the cause of thermoluminance observed by the researchers. Then he very cleverly fits this thermoluminance into his energy medicine frame work of ‘bioluminance’, vibrations, vital force, resonance and other pseudoscientific theories.
To be specific, precise and fitting to modern scientific knowledge system and its accepted paradigms, it is better to say ‘molecular imprints’ of original drug molecules are the cause of similarity of thermoluminance the researchers could observe. Such an explanation will clearly demonstrate that we are talking about the ‘complementary’ shape of drug molecules imprinted into nanostructures of water, which produce therapeutic effects by acting as ‘artificial binding sites’ for pathogenic molecules.
While introducing the concept of MIASMS, Hahnemann was actually trying to explain the role of residual effects of acute INFECTIOUS DISEASES in precipitating chronic disease conditions. His main focus was on infectious ITCH/LEPROSY, SYPHILIS and HPV-GONORRHOEA complex, which were most widespread around his place during his time.
Hahnemann, from his practical experience of applying ‘Similia Similibus Curentur’, came to the conclusion that complete cure is not possible using SIMILIMUM only, if such a similimum is selected using totality of currently existing symptoms only, without considering the MIASMS or residual effects of previous acute infectious diseases.
Even though Hahnemann could rightly observe the role of MIASMS or residual effects of infectious diseases in the causation as well as the curative process of chronic diseases, he could not explain the exact biological mechanism by which this phenomenon works. This failure was due to the primitive state scientific knowledge available during his period, which later led to various kinds unscientific and “dynamic” interpretations by his “disciples” and “followers” which continue till the present day.
Using the scientific knowledge already available now, I have been trying to explore the exact molecular mechanism by which residual effects of acute INFECTIOUS diseases contribute to the development of chronic disease conditions, which Hahnemann called MIASMS.
It is common knowledge that ANTIBODIES are generated in our body against infectious agents or proteins that are alien to our genetic codes. Even after infectious disease is over, these antibodies remain in our body for long periods, even for whole life in certain cases.
Since ANTIBODIES are native globulin PROTEINS that have undergone misfolding by interacting with alien proteins or infectious agents, they can themselves behave as aliens in the organism and produce pathological inhibitions by binding to various OFF-TARGET biological molecules. Such molecular inhibitions caused by ANTIBODIES are the real molecular level villains playing behind various chronic diseases such as AUTOIMMUNE DISEASES, PROTEINOPATHIES, AMYLOID DISEASES AND PRION DISEASES.
Hahnemann called these chronic residual effects of ANTIBODIES as MIASMS.
See, how Hahnemann’s concept of CHRONIC DISEASES relating it with INFECTIOUS MIASMS, paves the way for a SCIENTIFIC understanding of a whole class of grave diseases, and developing of a whole new range of therapeutic agents and techniques to combat them.
Hahnemann’s observations of CHRONIC DISEASES, relating it with INFECTIOUS DISEASES, would have been a revolutionary event in medical history, had anybody- be it hahnemann himself, his followers or scientists- taken up the task of explaining it in scientific terms.
Had anybody asked the question how an infectious disease can cause life-long RESIDUAL EFFECTS in the organism even after the infection is over, everything would have been clear. It would have been obvious that infectious agents can produce life-long RESIDUAL EFFECTS in the form of CHRONIC DISEASES only through ANTIBODIES generated in the body against infectious agents.
Such a realization would have helped medical as well as scientific community to view ANTIBODIES from a different perspective- as CAUSATIVE AGENTS of diverse types of CHRONIC DISEASES- over and above their role as DEFENSE molecules.
It was hahnemann, who for the first time proposed that diverse types of CHRONIC DISEASES could be produced in the long run by INFECTIOUS agents, which he called MIASMS.
I have been trying to explain in scientific terms, how CHRONIC DISEASES could be produced by infectious agents, even after the infections are over. This led me into the realization that INFECTIOUS AGENTS can produce life-long chronic disease dispositions only through OFF-TARGET actions of ANTIBODIES generated in the body against them.
By Chandran Nambiar KC
Without acquiring a baseline knowledge of CHEMISTRY OF LIFE, you cannot follow the MIT explanation regarding biological mechanism of homeopathic cure.
By the term ‘living organism’, we indicate a highly organized complex material system with a specific quantity, quality, structure and functions of its own, which is capable of self-controlled growth and reproduction of its progeny, through an interaction involving constant exchange of matter and energy with its environment.
The phenomenon we call ‘life’ exists through a continuous chain of highly complex biochemical interactions which control each other known as METABOLIC PATHWAYS, which depend up on each other and are determined by each other.
A ‘living organism’ represents a much higher and advanced level of organized existence of the same elements of matter we meet in the inorganic world, different only in its structural organization and functional complexity. The universal phenomenon of material motion we find as part of primary existence of matter itself, attains the wonderful qualities of life, due to this complex structural organization.
In fact, phenomenon of ‘life’ was the result of a continuous evolutionary process of primary matter in this universe through millions of years, attaining different levels of organizational and functional forms. Primary forces, sub-atomic particles, elementary atoms, simple chemical molecules, complex inorganic molecules, carbon containing organic molecules, bio-molecules, complex bio-polymers, RNA-DNA-Protein structures, organelles, unicellular organisms, multi-cellular organisms, diverse species of plants and animals, and ultimately Homo Sapiens- these are the prominent milestones in the known evolutionary ladder on earth, panning through millions and millions of years. Human beings represent the highest form of this material evolutionary history on earth, as far as it is known to us.
Parallel to this biological evolution, we can perceive a systematic evolution and perfection of the nervous system also. Simple forms of conditioned reflexes that existed in primitive organisms, gradually evolved into nerve cells, neural networks and ultimately into a well organized nervous system in higher animals. In higher forms of life such as humans, this nervous system has attained such a structural and functional perfection that human brain and its diverse faculties have begun playing a decisive role even in the existence and development of that species and even life on earth itself. Of course, collective labor, language and social relations also played a major role in this evolutionary process.
A living organism can exist only through a continuous interaction and material exchange with its environment. There is an unceasing flow of matter and energy in both directions, between internal and external environments of the organism. Metabolism, or ‘life process’ is the term used to describe the sum total of this bidirectional flow. The moment this bi-directional flow of matter and energy ceases, the organism can no longer exist.
A living organism is distinguished from other non-living forms of matter by certain fundamental features such as: high level of structural organization, the ability to convert and utilize energy, continuous material exchange with environment, self regulation of chemical transformations, and, reproduction or transfer of hereditary information. A state of disease may ensue when any of the biochemical pathways governing these fundamental factors of life are disturbed. Obviously, it is impossible to make a scientific study of pathology and therapeutics without an understanding of these subjects.
Complex bio-molecules which participate in the diverse chemical processes of life are broadly classified into four major groups: Proteins, Carbohydrates, Lipids and Nucleic Acids. These are polymers of simple chemical components or sub units, called monomers. The monomers of proteins are amino acids, and those of carbohydrates are monosaccharides. Lipids are polymers of fatty acids. The monomers of Nucleic acids are known as nulcleotides. These bio-molecules are considered to be the building blocks of life on earth, and are never seen in the non-living world. These bio-molecules, with their highly complex structure and organization, interact each other in the organism through hundreds of bio-chemic pathways, collectively called ‘vital processes’.
Scientific explanation of Homeopathy should be based on a proper understanding of the the complex dynamics of bio-molecular interactions involved in vital processes, especially protein biochemistry.
Understanding PROTEIN CHEMISTRY and PROTEIN DYNAMICS is an essential part of understanding LIFE, DISEASE and CURE:
Proteins are a class of highly complex nitrogen-containing bio-molecules, functioning as the primary carriers of all the biochemical processes underlying the phenomenon of life. There exist millions of protein molecules belonging to thousands of protein types in a living organism.
Each protein molecule is formed by the polymerization of monomers called amino acids, in different proportions and sequences. Each protein type has its own specific role in the biochemical interactions in an organism. Most of the amino acids necessary for the synthesis of proteins are themselves synthesized from their molecular precursors inside the body. A few types of amino acids cannot be synthesized inside the body, and have to be made available through food. These are called essential aminoacids.
There are specific protein molecules assigned for each biochemical process that take place in the body. Various proteins play different types of roles, such as biological catalysts or enzymes, receptors, transport molecules, hormones, antibodies etc. Some proteins function as specialized molecular switches, systematically switching on and off of specific biochemical pathways.
Proteins are synthesized from amino acids, in conformity with the neucleotide sequences of concerned genes, with the help of enzymes, which are themselves proteins.
‘Protein synthesis’ and ‘genetic expression’ are very important part of vital process. It may be said that genes are molecular moulds for synthesizing proteins of specific conformations. There are specific genes, bearing appropriate molecular codes of information necessary for synthesizing each type of protein molecule. Even the synthesis of these genes happens with the help of various enzymes, which are protein molecules. There is no any single bio-molecular process in the living organism, which does not require an active participation of a protein molecule of any kind.
The most important factor we have to understand while discussing proteins is the role of their three-dimensional spacial organization evolving from peculiar disulphide bonds and hydrogen bonds. Water plays a vital role in maintaining the three dimensional organization of proteins intact, thereby keeping them efficient to participate in the diverse biochemical processes.
Proteins exhibits different levels of molecular organization: primary, secondary, tertiary and quaternary. It is this peculiar three dimensional structure that decides the specific biochemical role of a given protein molecule. More over, co-enzymes and co-factors such as metal ions and vitamins play an important role in keeping up this three-dimensional structure of protein molecules intact, thereby activating them for their specific functions. Buffering properties of body fluids also are decisive in maintaining the specific conformations of proteins and keeping them reactive.
Whenever any kind of error occurs in the particular three-dimensional structure of a given protein molecule, it obviously fails to interact with other biomolecules to accomplish the specific functions it is intended to play in the concerned biochemical processes. Such a failure leads to further harmful deviations in several biochemical processes in the organism, that require the participation of this particular protein, ultimately resulting in a cascading of multitude of molecular errors. This is the fundamental molecular mechanism of pathology, which we perceive as disease of some or other category.
These deviations in biochemical pathways are expressed as various groups of subjective and objective symptoms of disease. The organic system exhibits a certain degree of ability and flexibility to overcome or self repair such molecular deviations and preserve the state of homeostasis required to maintain life. Anyhow, if these deviations happen in any of the vitally decisive biochemical pathways, or, if these are irreversible, the bio-chemical processes ultimately stop and death happens.
Disease is a state of derangement in biochemical interactions so as to disrupt the normal pathways of vital processes of the organism
Derangement in normal biochemical interactions amounting to a state of disease may happen due to diverse reasons.
1. GENETIC FACTORS: Defects in genetic codes arising from heredity or acquired by mutations result in the absence of certain proteins (enzymes, receptors, antibodies etc) that are essential for normal biochemical interactions.defective genes may also synthesis faulty proteins with wrong conformation, which can act as endogenous pathogenic agents by binding to various biological targets.
2. EPIGENETIC FACTORS: Defects of enzymes involved in genetic expressions and post synthetic translations and modifications of protein molecules act as epigenetic factors of diseases.
3. NUTRITIONAL FACTORS: Nutritional deficiencies of essential building blocks and precursors of biological molecules, such as amino acids and other monomers, vitamins, co-factors, elements, metal ions, minerals etc may disrupt the normal biochemical interactions. Any shortage in the availability of various amino acids and their precursers may lead to non- production of essential proteins in the organism. In some cases, it may also result in the production of defective proteins.
4. ENVIRONMENTAL FACTORS: Biochemical interactions happen only if an appropriate pH level and temperature is maintained in the body fluids. Any physical influence that may derange these physical parameters will act as pathogenic factors by deactivating protein molecules. Temperature, magnetic field, electromagnetic radiations, vibrations and various other physical influences can affect the normal biochemical processes. Physical influences actually act as pathogenic agents by producing derangement in protein conformations, which are deactivated or converted to pathogenic molecules.
5. EXOGENOUS MOLECULAR FACTORS: Chemical molecules released by infectious agents invading the organism, drugs, toxins, food articles, environmental pollutants alien proteins entering the body act as EXOGENOUS factors of disease by binding to various biological molecules such as enzymes and receptors and producing molecular inhibitions.
6. ENDOGENOUS MOLECULAR FACTORS: Antibodies, hormones, neuro-mediators, neurotransmitters, cytokines, growth factors, super-oxides, enzymes and various biological molecules of endogenous origin may cause molecular inhibitions of proteins such as enzymes and receptors, thereby acting as pathogenic agents.
It is obvious that almost all conditions of pathology we normally confront, including those resulting from genetic origin, are involved with some or other errors or absence of some protein molecules that are essential for concerned biochemical processes.
Moreover, most of such molecular errors other than of nutritional deficiencies or genetic origin, arise due to binding of some exogenous or endogenous foreign molecules or ions on the active, binding or allosteric sites of protein molecules, effecting changes in their three-dimensional conformations. A host of diseases originating from viral-bacterial infections, allergies, poisoning, drugs, food articles etc, belong to this category. Chronic diseases caused by antibodies, which are considered in homeopathy as miasmatic diseases and modern medicine as auto-immune diseases, also belong to this class. Diseases caused by emotional factors, hormones, neuro-mediators, neurotransmitters, cytokines, growth factors, super-oxides, enzymes and various biological molecules also include in this group.
KEY-LOCK MECHANISM: The most important factor we have to bear in mind when talking about kinetics of proteins in general, and enzymes in particular is their highly defined, peculiar specificity. Each type of protein molecules, or some times even some part of a single protein molecule, is designed in such a way that it can bind only with a specific class of molecules, and hence participate in a specific type of bio-chemic interaction only. This functional specificity is ensured through the peculiar three-dimensional configuration of the protein molecules, exhibited through their characteristic folding and spacial arrangement. Reactive chemical groups known as active sites, binding sites, and regulatory sites are distributed at specific locations on this three dimensional formations of protein molecules. These chemical groups can interact only with molecules and ions having appropriate spacial configurations that fits to their shape. This phenomenon can be compared with the relationship existing between a lock and its appropriate key. Just as a key with an exactly fitting three dimensional shape alone can enter the key hole of a lock and open it, molecules with exactly fitting three dimensional structure alone can establish contact and indulge in chemical activities with specific protein molecules. This key-lock relationship with substrates defines all biochemical interactions involving proteins, ensuring their optimum specificity. Obviously, any deviation in the three dimensional configuration of either lock or key makes their interaction impossible.
It has been already explained that the primary basis of any state of pathology is some deviations occurring in the biochemical processes at the molecular level. Endogenic or exogenic foreign molecules or ions having any configurational similarity to certain biochemical substrates can mimic as original substrates to attach themselves on the regulatory or the active sites of proteins, effecting changes in their native 3-D configuration, thereby making them unable to discharge their specific biochemical role. This situation is called a molecular inhibition, which leads to pathological molecular errors. It is comparable with the ability of objects having some similarity in shape with that of key, to enter the key hole of a lock and obstructing its function. As a result of this inhibition, the real substrates are prevented from interacting with the appropriate protein molecules, leading to a break in the normal biochemical channels. This type of molecular errors are called competitive inhibitions. It is in this way that many types of drugs, pesticides and poisons interfere in the biochemical processes, creating pathologic situations. Such substances are known as anti-melabolities.
To understand the ridiculous foolishness involved in the claims regarding distribution of homeopathic medicine Arsenic Album 30 as IMMUNE BOOSTERS against covid 19, we should first of all learn what is IMMUNITY. Most disappointing thing is that most of our homeopaths are not bothered about such a learning.
In a scientifically conscious and watchful community, we cannot talk about IMMUNE BOOSTING using homeopathic medicines without explaining the biological mechanism by which such a phenomenon works. We have to be ready to face obvious hard questions.
From the ongoing discussions below, you will understand that you cannot produce IMMUNITY against particular disease without inducucing production of ANTIBODIES against the specific pathogens. It is a matter of basic scientific knowledge that production of antibodies will happen only if we introduce into the body some protein molecules that are ALIEN to the genetic blueprint of the organism. Everybody knows ASENICUM ALBUM 30 does not contain any such molecules having antigenic properties, and as such, claiming to boost immunity using that preparation is totally baseless.
What we call IMMUNITY is actually a complex biological system functioning in living organisms, endowed with the capacity to recognize and tolerate whatever belongs to the SELF, and to recognize and reject
what is non-self or ALIEN to its genetic blueprint.
IMMUNITY is the capability of multicellular organisms to resist harmful microorganisms invading our body. Immunity involves both specific and nonspecific components. The NONSPECIFIC components act as barriers or eliminators of a wide range of pathogens irrespective of their antigenic make-up. SPECIFIC components of the immune system adapt themselves to each new disease encountered and can generate pathogen-specific immunity.
The immune system has two components: innate and adaptive immunity. The innate immunity is present in all animals, while the adaptive immunity occurs only in vertebrates.
The innate system involves the biological mechanism for recognition of certain ALIEN molecules and stimulating of two types of innate immune responses against them, such as inflammatory responses and phagocytosis.
The adaptive immune system, on the other hand, is composed of more advanced lymphatic cells that are programmed to distinguish between specific “non-self” or alien substances in the presence of “self”. The reaction to foreign substances is etymologically described as inflammation, meaning to set on fire.
Actually, IMMUNITY is the ‘non-reaction’ or ‘exemption’ towards “self” substances.
These innate and adaptive components of the immune system create a dynamic biological environment where “health” can be seen as a physical state where the self is immunologically spared, and what is foreign is inflammatorily and immunologically eliminated.
A state of “disease” can arise when our immune system fails to eliminate ‘alien’ substances, or spare what is ‘self’.
Innate immunity, also known as native immunity, is a semi-specific form of immunity, considered as the first line of defense against pathogens, representing a critical systemic response to prevent infection and maintain homeostasis, and contributing to the activation of an adaptive immune response.
Innate immune system does not adapt to specific external stimulus or a prior infection, but relies on genetically encoded recognition of particular molecular patterns.
Adaptive immunity is also known as acquired immunity. It is the active component of the host immune response, and is mediated by antigen-specific lymphocytes.
Unlike the innate immunity, the acquired immunity is highly specific to a particular pathogen, including the development of immunological memory. Similar the innate system, the acquired system includes both humoral immunity components and cell-mediated immunity components.
Adaptive immunity can be acquired either ‘naturally’ by infection, or ‘artificially’ through deliberate actions such as vaccination. it is associated with molecular memory of the pathogen.
Adaptive immunity is classified as ‘active’ or ‘passive’.
Active immunity is acquired through the exposure to a pathogen, which triggers the production of antibodies by the immune system.
Passive immunity is acquired through the transfer of antibodies or activated T-cells derived from an immune host either artificially or through the placenta; it is short-lived, requiring booster doses for continued immunity.
A drug substance becomes CONSTITUTIONAL MEDICINE of an individual, if it contains one or more types of chemical molecules which can “compete” with the pathogenic molecules that have produced molecular inhibitions in diverse types of biological targets causing errors in various important biochemical pathways, that are expressed through diverse trains of symptoms that belong to the classes considered to be ‘physical’ and ‘mental’ generals.
In post-avogadro dilutions, this CONSTITUTIONAL MEDICINE will contain molecular imprints of the chemical molecules contained in them, which can act as artificial binding pockets for the pathogenic molecules due to their conformational affinity, deactivate them, and remove the pathological molecular inhibitions they have produced in the body.
CONSTITUTIONAL SYMPTOMS are the expressions of disruptions in METABOLIC PATHWAYS- both anabolic as well as catabolic. These disruptions happen mainly due to inhibitions of enzymes involved in the biochemical processes in metabolic pathways caused by binding with diverse types of exogenous or endogenous pathogenic molecules. Metabolic pathways may also be disrupted due to reasons such as nutritional non-availability of essential molecules and metabolites, scarcity or over expressions of signalling molecules such as hormones and cytokines etc, which are also related with inhitions of related with their genetic expressions.
A metabolic pathway is a series of interdependent biochemical reactions controlled by enzymes occurring within a cell. The reactants, products, and intermediates of an enzymatic reaction are known as metabolites, which are modified by a sequence of chemical reactions catalyzed by enzymes. In most cases of a metabolic pathway, the product of one chemical reaction catalyzed by a particular enzyme acts as the substrate for the next. These enzymes often require dietary minerals, vitamins, and other cofactors to function. Side products of these reactions are considered waste, and normally removed from the cell.
Different metabolic pathways take place based on the position within a eukaryotic cell and the significance of the pathway in the given compartment of the cell. For instance, the, metabolic pathways such as electron transport chain, and oxidative phosphorylation etc take place in the mitochondrial membrane. Glycolysis, pentose phosphate pathway, and fatty acid biosynthesis etc occur in the cytosol of a cell.
There are two types of metabolic pathways:
ANABOLIC pathways are characterized by their ability to either synthesize molecules with the utilization of energy.
CATABOLIC pathways are involved with break down of complex molecules by releasing energy in the process.
The two pathways complement each other in that the energy released from one is used up by the other. The degradative process of a catabolic pathway provides the energy required to conduct a biosynthesis of an anabolic pathway. In addition to the two distinct metabolic pathways there is the amphibolic pathway, which can be either catabolic or anabolic based on the need for or the availability of energy.
Metabolic pathways are required for the maintenance of HOMEOSTASIS within an organism, and the flux of metabolites through a pathway is regulated depending on the needs of the cell and the availability of the substrate.
The end product of a metabolic pathway may be used immediately, initiate another metabolic pathway or be stored for later use. The metabolism of a cell consists of an elaborate network of interconnected pathways that enable the synthesis and breakdown of molecules.
Each metabolic pathway consists of a series of biochemical reactions that are connected by their intermediates. The products of one reaction are the substrates for subsequent reactions, and so on. Metabolic pathways are often considered to flow in one direction. Although all chemical reactions are technically reversible, conditions in the cell are often such that it is thermodynamically more favorable for flux to proceed in one direction of a reaction. For example, one pathway may be responsible for the synthesis of a particular amino acid, but the breakdown of that amino acid may occur via a separate and distinct pathway.
Glycolysis was the first metabolic pathway discovered. As glucose enters a cell, it is immediately phosphorylated by ATP to glucose 6-phosphate in the irreversible first step. In times of excess lipid or protein energy sources, certain reactions in the glycolysis pathway may run in reverse to produce glucose 6-phosphate, which is then used for storage as glycogen or starch.
Metabolic pathways are often regulated by feedback inhibition.
Some metabolic pathways flow in a ‘cycle’ wherein each component of the cycle is a substrate for the subsequent reaction in the cycle, such as in the Krebs Cycle.
Anabolic and catabolic pathways in eukaryotes often occur independently of each other, separated either physically by compartmentalization within organelles or separated biochemically by the requirement of different enzymes and co-factors.
A CATABOLIC PATHWAY is a series of reactions that bring about a net release of energy in the form of a high energy phosphate bond formed with the energy carriers adenosine diphosphate (ADP) and guanosine diphosphate (GDP) to produce adenosine triphosphate (ATP) and guanosine triphosphate (GTP), respectively. The net reaction is, therefore, thermodynamically favorable, for it results in a lower free energy for the final products. A catabolic pathway is an exergonic system that produces chemical energy in the form of ATP, GTP, NADH, NADPH, FADH2, etc. from energy containing sources such as carbohydrates, fats, and proteins. The end products are often carbon dioxide, water, and ammonia. Coupled with an endergonic reaction of anabolism, the cell can synthesize new macromolecules using the original precursors of the anabolic pathway. An example of a coupled reaction is the phosphorylation of fructose-6-phosphate to form the intermediate fructose-1,6-bisphosphate by the enzyme phosphofructokinase accompanied by the hydrolysis of ATP in the pathway of glycolysis. The resulting chemical reaction within the metabolic pathway is highly thermodynamically favorable and, as a result, irreversible in the cell.
Cellular respiration is a core set of energy-producing catabolic pathways occuring within all living organisms in some form. These pathways transfer the energy released by breakdown of nutrients into ATP and other small molecules used for energy (e.g. GTP, NADPH, FADH). All cells can perform anaerobic respiration by glycolysis.
Additionally, most organisms can perform more efficient aerobic respiration through the citric acid cycle and oxidative phosphorylation. Additionally plants, algae and cyanobacteria are able to use sunlight to anabolically synthesize compounds from non-living matter by photosynthesis.
In contrast to catabolic pathways, ANABOLIC PATHWAYS require an energy input to construct macromolecules such as polypeptides, nucleic acids, proteins, polysaccharides, and lipids. The isolated reaction of anabolism is unfavorable in a cell. Thus, an input of chemical energy through a coupling with an exergonic reaction is necessary. The coupled reaction of the catabolic pathway affects the thermodynamics of the reaction by lowering the overall activation energy of an anabolic pathway and allowing the reaction to take place. Otherwise, an endergonic reaction is non-spontaneous.
An anabolic pathway is a biosynthetic pathway, meaning that it combines smaller molecules to form larger and more complex ones. An example is the reversed pathway of glycolysis, otherwise known as gluconeogenesis, which occurs in the liver and sometimes in the kidney to maintain proper glucose concentration in the blood and supply the brain and muscle tissues with adequate amount of glucose. Although gluconeogenesis is similar to the reverse pathway of glycolysis, it contains three distinct enzymes from glycolysis that allow the pathway to occur spontaneously.
1. Feedback from Dr. Suresh S Patel. Om Shree clinic, opp: Gawara tower, Mochiwad Road, Khambhat. Gujarat.388620, Ph: 9879062647, regarding his experience with MIT formulation CEPHAMIT in the treatment of chronic MIGRAINE:
“A female patient, Age: 38 yrs. Migraine type headache since last 3yrs. Every 15 to 20 days repeats the attack. Pain in one side of skull, with vomiting & feeling of nausea. Has been taking painkillers & anti-migraine tabs & Tranquilizers, but only temporarily relief. Gave Nat.Mur 1M one dose, and
MIGROMIT 10drops tid . 2 bottles of migromit completed, till date no occurrence of headache. Patient feel very well. Thanks MIT formulation.”
2. Feedback from Dr.Pulkit Gupta, Homoepathic clinic, Aghwanpur, moradabad, Uttarpradesh,
+91 96544 99884, regarding his experience with MIT formulation
“Patient a child of aged 6 years of age, suffering from broncho spasmodic cough with vomiting since 2-3 days. I started with BRONCHOMIT 10 drops 3 times a day with indicated remedy. All the cough symptoms was no more. Child started playing as usual which he used to. Thanks to MIT.”
3. MIT IN PERSISTENT COUGH:
Feedback from Dr Arshad pathan, Life Care Clinic, Bus stand, Ambua, Alirajpur, Madhya pradesh, Ph 7869230555, regarding his experience with MIT formulation BRONCHOMIT in a case of persistent COUGH.
“Male patient, age 53 years, suffering from cough since 5-6 months. Taken treatment from various doctors ( including chest physician). All investigations where normal, includind x ray.
Patient came to me. Chest was clear and no any abnormal sounds. I started with BRONCHOMIT 5 drops tds then in just 4 days there is no cough…”
4. MIT IN LUMBOSACRAL SPONDYLOSIS
A feedback from Dr Manisha Deshmukh, Pune, Maharashtra, Ph: 98221 18479, regarding her experience with MIT formulations in a case of LUMBOSACRAL SPONDYLOSIS:
“A 62 yrs old female patient, suffering from Cervical and Lumbosacral spondylosis since 2 years
Had visited my hospital on 20th Jan 2020. Was given Spinomit and spondomit 10 drops bd for 2 months
Later she visited us on 10th Apr 20 informing all symptoms cleared.
On 1st Sep 20, patient reported for mild pain in left leg and pain in Lt knee joint
She was prescribed Spinomit, Arthromit and Gerimit 10 drops bd for 15 days, after she is fine till date with no complaints”
5. Feedback from Dr Arshad pathan, Life Care Clinic, Bus stand, Ambua, Alirajpur, Madhya pradesh, Ph 7869230555, regarding his experience with MIT formulations GYNOMIT and AMENMIT in a case of AMENORRHEA:
“Female patient, age 40, came to me with c/o amenorrhea since 6 months. All investigations were normal ( usg, blood reports and harmonal reports). Also taken treatment from many gynecologists. But there is no any result.
I started with with GYNOMIT and AMENMIT. Within just 1 month normal mentrual cycle came…”
6. Feedback from Dr.Pulkit Gupta, Homoepathic clinic, Aghwanpur, moradabad, Uttarpradesh,
+91 96544 99884, regarding his experience with MIT formulation ARTHROMIT:
“Female patient aged 48 years was complaining of joint pain since 2-3 years. I started with ARTHROMIT, 10 drops 3 times a day for 2 weeks. Joint pain was no more, thanks to MIT protocol.
I have also tried PYROMIT, DYSMENMIT etc in other cases, and all worked well. Thankyou sir.”
7. A feedback from Dr Manisha Deshmukh, Pune, Maharashtra, Ph: 98221 18479, regarding her experience with MIT formulations ALLERMIT and RHINMIT:
“A lawyer aged 28 yrs, was suffering from allergic rhinitis since August 2019, reported in my clinic on 18th November 2020.
Allermit and Rhinimit 10 drops bd was dispensed.
Surprisingly she has called me on 21st November, informing me about all symptoms of allergic rhinitis gone.
Thank you Chandran Nambiar sir, for introducing me to this wonderful system of medicine in a scientific way.
Looking forward for more such patients to be getting cured in our clinic.”
8. Here is a great feedback from Dr.G.Madhu sudhan Bsc.BHMS, Balaji clinic, Hoskote, Bangalore, 9980509963, regarding his experience with MIT formulation CEPHAMIT in chronic headache:
“CEPHAMIT has excellent result in headache.
A Lady aged 39 years consulted me for her complaint of headache. Headache since 2 to 3 years. Took treatment for the same…she tried allopathy..ayurveda…even homeopathy…but no permanent relief. She was fedup with all these things..she relied on croc in..anacin..or paracetamol like analgesics..
She came to me without much confidence… first I ruled out is there any sinus problem & then I send her for eye testing..nothing wrong in that..and checked for BP to rule out hypertension & blood check up for hormonal changes…everything is alright..she is from well settled family..no financial burden..no anxiety…no sleeping problems.(.sleep disturbance is there because of headache..once if she takes analgesics that is also ok).
I simply prescribed CEPHAMIT 10drops BD.
She got relief within 8days. Suggested to continue for one month. In between that frequency of episodes of her headache reduced, and having sound sleep also. From last 2 months she had not took single analgesic.
Really CEPHAMIT is an excellent remedy for headache. Thank you sir.”
9. Dr Manojkumar Chajjed, Nashik, Maharastra ph- 7588037280 writes about his experience with MIT formulation CEPHAMIT :
“A Female 20 year old , 43kg, had severe Head pain during lockdown time April. She can’t sleep. She cunsulted Physician but not get relief. I give CEPHAMIT 10 drops tds. Within 10 day she got relief.
She has till now no any complaint about head pain in routine working.
Really MIT FORMULATIONS work wonderful. Thank you Sir ”
10. Feedback from Dr.Redage Sumit B.
BHMS, Nashik, Maharashtra, Ph- +91 95273 74951, regarding his experience with MIT formulation ARTHROMIT in a case of OSTEOARTHRITIS:
“A 30 years old lady having c/o joint pain treated with Arthromit. #Promising Result with Scientific Homoeopathy
“I have been suffering from joint pain for the last 1 year. Even taking a lot of pain Killers didn’t alleviate the problem. It also made it difficult for me to do my daily chores. Finally I took Homoeopathic treatment from Dr.Redage Sir. Within 4 days of starting medication I started to feel better. Now I can manage my pain without a single painkiller. Now I can also do my daily work. Thank you Doctor.”
Arthromit 5 drops (in tsp water) × TDS for 15 days
11. A feedback from Dr Partha Ghosh, Siliguri,West Bengal, ph- 8250487994, regarding his experience with MIT formulations BRONCHOMIT in a chronic BRONCHITIS patient:
“Male retired Govt employee, age 61, male. Service time was smoker. Bronchitis patient. Tremendous problem of breathing asthama
After BRONCHOMIT, he is now totally ok, where allopathy plus hospitalized conditions occurred earlier. Now no complaints. Excellent MIT!”
Patients around West Bengal may contact Dr Partha Ghosh over 8250487994 for expert treatment according to MIT PROTOCOL.
He has got a good stock of MIT FORMULATIONS. Doctors can contact him for knowing more about their use and buying them.
12. A feedback from Dr Partha Ghosh, Siliguri,West Bengal, ph- 8250487994, regarding his experience with MIT formulations BRONCHOMIT in a chronic BRONCHITIS patient:
“Male retired Govt employee, age 61, male. Service time was smoker. Bronchitis patient. Tremendous problem of breathing asthama
After BRONCHOMIT, he is now totally ok, where allopathy plus hospitalized conditions occurred earlier. Now no complaints. Excellent MIT!”
13. A feedback from Dr Dattaraj, Goa, 97645 99530, regarding his experience with MIT formulations BRONCHOMIT and PULMOMIT in relieving a case of acute ASTHMA:
“Hello Sir, I did a home visit of 55yrs old female. Presented with severe wheezing since yesterday night. Spo2 80% , RS- B/L Rhonchi. I had given BRONCHOMIT 10drops with PULMOMIT 10drops every 15mins. Plus steam inhalation by adding 10 drops of both.
Pt improved drastically. Spo2 from 80% came to 94% within 1/2hour.”
14. Dr Alokesh Bhattacharya, Hooghly, West Bengal, Ph- 91 93309 49695, has shared a feedback regarding his experience with MIT FORMULATIONS:
“Good morning sir. I would like to share an outstanding successful case of dysmenorrhoea treatment wit MIT FORMULATIONS.
Patient was suffering from dysmenorrhoea since her menerche. Now she is 24 yrs. Unmarried . She has tremendous maddening pain from 1st day of period to 5th day.
She was always taking diclofenac
for this complaint, though she was taking constitutional homoepathic medicine as well as palliative homoeopathic medicine during pain without any effect. And she was bound to take analgesics.
But this time she took ALGIMIT AND DYSMENMIT alternately for 5days during her period, and she required no analgesic. Its great success.
I have also got good results from ALLERMIT, ALGIMIT and PYROMIT in different cases”.
15. Feedback from Dr Partha Ghosh, Siliguri, West Bengal, Ph- 8250487994, regarding his experience with the MIT formulation SPONDOMIT:
Patient a female house wife. Cervical spondilysis last 20 years, after birth of her first male child. Stiffness of neck associated with back pain, hand pain and vertigo. They were regular symptoms. Gave ALGIMIT and SPONDOMIT. Within 2 days no pain. Regular work. Now she is coming to me with old songs in singing, that I am completely fine.”
Great mit formulations!”
16. Dr Pravin Prajapati , Mehsana, Gujarat, phone +91 97233 95545, writes about his experience with MIT FORMULATIONS :
“A Female 50 year old , diabetes, over weight, 90 kg, had severe lumbar pain during lockdown time April. She can’t sleep. She cunsulted two orthopaedic Doctors within 10 day but no relief. Then I have gave her SPINOMIT and ALGIMIT. She got a relief from pain within 2 days. 10 drop 6 time. After 2 day 4 time 10 drop. To 15 day.
She has till now no any complaint about lumbar pain in routine working.
I HAVE GOT WONDERFUL RESULTS IN COLD , FEVER FROM ‘CORYMIT’ AND ‘PYROMIT’ during this VIRAL SEASON
in many patients.
I have also got results in allergic respiratory complaints from ALERMIT in MANY PATIENTS.
Really MIT FORMULATIONS work wonderfully.”
17. Feedback from Dr Sandeep Selvinus MD, Andhrapradesh, ph- 99488 41285, regarding his experience with IBSMIT in the treatment of IRRITABLE BOWEL SYNDROME:
“I am Grateful to you for providing such a good combination. A patient of mine suffering from IBS problem since 2 yrs got her problem recovered 80% within 1month after I prescribed “IBSMIT” alone only .
Thank you sir,
Dr.sandeep selvinus, M.D
How can you discuss “MODUS OPERANDI” of Arsenic Alb 30 or any other post-avogadro diluted homeopathic drug, without discussing regarding the ACTIVE PRINCIPLES they contain?
MIT or MOLECULAR IMPRINTS THERAPEUTICS is a scientific hypothesis trying to explain homeopathy.
As per this hypothesis, potentization involves a process of Molecular Imprinting in water-alcohol supra-molecular matrix using drug molecules as templates, by which nanocavities or molecular imprints bearing the spacial conformations of drug molecules in a negative orientation are produced. Drugs potentized above avogadro limit contain these MOLECULAR IMPRINTS as their active principles, which can act as artificial binding pockets for the pathogenic molecules.
One of the main criticisms against this hypothesis was that molecular imprinting could be done only in POLYMERS, and since water is not a polymer, molecular imprinting could not be done in water-alcohol matrix. Even though I had scientifically explained why water is considered a polymer-like substance, many people were reluctant to accept my explanations. Now comes a great research work that has scientifically proved that “Liquid water is a dynamic polydisperse branched polymer. This work done by a team led by William A. Goddard III and Saber Naserifar is a great breakthrough in water research, which will of course be of course a decisive help in establishing THE concept MOLECULAR IMPRINTING involved in homeopathic potentization as hypothesised by MIT.
According to the researchers, they have proved through quantum mechanics force field molecular simulations that Liquid water is a dynamic polydisperse branched polymer. They have showed that when ice undergoes melting, the number of SHBs (strong hydrogen bonds) drops quickly to two in liquid water. These two SHBs couple into chains containing over 150 water molecules, resembling a branched polymer, where polymer branches evolve dynamically. Authors expect that this dynamics-branched polymer paradigm may explain long-standing puzzles of water, and may explain the observed angular correlations in water.
You can read the research paper on this link: .https://www.pnas.org/content/116/6/1998
I have before me a research paper titled “covid-19 research Homoeopathy- Efficacy of Arsenicum Alb 30c for upregulating immunological markers among residents of covid-19 related hot spot areas in Pathanamthitta, Kerala”, recently published by Dr M V Thomas and coworkers, including some of the senior homeopaths from kerala.