Homeopathy Is Molecular Imprints Therapeutics (MIT)- An advanced branch of modern molecular medicine. Only difference between molecular medicine and MIT is that where as molecular medicine uses ‘drug molecules’ as therapeutic agents, MIT uses ‘molecular imprints’ of drug molecules.
Reading this title, even my most optimistic homeopath friends would accuse me of making an over-exaggerated and far extended claim about homeopathy. They would wonder how I dare to relate homeopathy with modern molecular medicine, which according to them are mutually incompatible and inimical. For scientific people it would be difficult even to imagine how a 250 year old and still unproved therapeutic system such as homeopathy could be claimed to be an advanced medical discipline.
Homeopathy is considered by the scientific community as a nonsense theory based on unscientific philosophy of vitalism, where as the proponents of homeopathy still try to explain and market it as a ‘spiritualistic’ healing art.
In this peculiar intellectual context, I am aware it will be extremely difficult for both scientific community as well as homeopathic community to accept my claim that homeopathy is an ‘advanced branch of modern molecular medicine’. I will have to struggle much to present the logic behind my statement in a convincing way.
If anybody asks me to explain what is homeopathy, I would prefer to say it is MIT or Molecular Imprints Therapeutics. I think that reply would specifically define in minimum words my scientific meaning of ‘similia similibus curentur’, the fundamental therapeutic principle of homeopathy.
If I am asked to explain further, now I am confident enough to say it is a higher specialized branch of modern Molecular Medicine. It is based on the therapeutic principle of ‘similia similibus curentur’, which scientifically means “endogenous or exogenous pathogenic molecules that cause diseases by binding to the biological molecules can be entrapped and removed using molecular imprints of drug molecules which in molecular form can bind to the same biological molecules, utilizing the complementary configurational affinity between molecular imprints and pathogenic molecules”.
My claim of homeopathy as a specialized branch of modern molecular medicine evolves from my understanding of homeopathic potentization as a process of molecular imprinting. Conventionally, molecular imprinting is a technology of preparing three dimensional artificial binding sites for molecules in polymer matrixes, which are widely used in many biological assays, molecular separation protocols and many other laboratory applications. From studying the ‘polymer-like’ behavior of water in its ‘supra-molecular’ structural level, I am fully convinced that water, especially water-ethyl alcohol mixture can also be used as a medium for molecular imprinting similar to polymers, and the ‘molecular imprints’ thus produced can be safely used as therapeutic agents. They would act as selective artificial binding sites for pathogenic molecules. In my opinion, this phenomenon of molecular imprinting is involved tin homeopathic potentization, and the active principles of potentized drugs are ‘molecular imprints’ of drug molecules.
Through this definition, potentization becomes a branch of modern drug designing technology, and homeopathy becomes branch of modern molecular medicine.
Molecular medicine is the most advanced, most scientific and recently originated discipline in modern medical science. It is a broad field, where physical, chemical, biological and medical techniques are used to describe molecular structures and mechanisms, identify fundamental molecular and genetic errors of pathology, and to develop molecular interventions to correct those errors.
The molecular medicine perspective emphasizes cellular and molecular phenomena and interventions rather than the previous conceptual and observational focus on patients and their organs.
History of modern molecular medicine is very recent in origin. The groundwork for establishing the field of molecular medicine is considered to be laid in 1949, with a paper on “Sickle Cell Anemia, a Molecular Disease” published in Science magazine by Linus Pauling, Harvey Itano and others. In 1956, Roger J. Williams wrote Biochemical Individuality,a prescient book about genetics, prevention and treatment of disease on a molecular basis. Another paper in Science by Pauling in 1968,introduced and defined this view of molecular medicine that focuses on natural and nutritional substances used for treatment and prevention.
‘Biological revolution’ of 1970s gave great impetus to molecular medicine perspective, and led to the introduction of many innovative techniques and commercial applications.
Now, Molecular medicine is a new scientific discipline in many medical universities. Combining contemporary medical studies with the field of biochemistry, it offers a bridge between the two subjects. At present only a handful of universities offer the course to undergraduates. With a degree in this discipline the graduate is able to pursue a career in medical sciences, scientific research, laboratory work and postgraduate medical degrees.
Molecular Medicine covers research on molecular pathogenesis of disease and translation of this knowledge into specific molecular tools for diagnosis, treatment, and prevention.
‘Molecular pathology’ and ‘proteomics’ are emerging disciplines associated with molecular medicine, and focuses in the study and diagnosis of disease through the examination of ‘molecules’ within organs, tissues or bodily fluids. Molecular pathology shares some aspects of practice with both anatomic pathology and clinical pathology, molecular biology, biochemistry, proteomics and genetics, and is sometimes considered a “crossover” discipline. It is multi-disciplinary in nature and focuses mainly on the sub-microscopic aspects of disease and unknown illnesses with strange causes.
It is a scientific discipline that encompasses the development of molecular and genetic approaches to the diagnosis and classification of various human diseases, the design and validation of predictive biomarkers for treatment response and disease progression, the susceptibility of individuals of different genetic constitution to develop cancer, and the environmental and lifestyle factors implicated in pathogenesis.
Exactly, ‘proteomics’ is the basis of ‘molecular pathology’. ‘Proteomics’ is the large-scale study of proteins, particularly their structures and functions. Proteins are vital parts of living organisms, as they are the main components of the physiological metabolic pathways of cells. The term “proteomics” was first coined in 1997 to make an analogy with genomics, the study of the genes. The word “proteome” is a blend of “protein” and “genome“, and was coined by Marc Wilkins in 1994. The proteome is the entire complement of proteins, including the modifications made to a particular set of proteins, produced by an organism or system. This will vary with time and distinct requirements, or stresses, that a cell or organism undergoes. After genomics, proteomics is considered the next step in the study of biological systems. It is much more complicated than genomics mostly because while an organism’s genome is more or less constant, the proteome differs from cell to cell and from time to time. This is because distinct genes are expressed in distinct cell types. This means that even the basic set of proteins which are produced in a cell needs to be determined.
Scientists are very interested in proteomics because it gives a much better understanding of an organism than genomics. First, the level of transcription of a gene gives only a rough estimate of its level of expression into a protein. An mRNA produced in abundance may be degraded rapidly or translated inefficiently, resulting in a small amount of protein. Second, as mentioned above many proteins experience post-translational modifications that profoundly affect their activities; for example some proteins are not active until they become phosphorylated. Methods such as phosphoproteomics and glycoproteomics are used to study post-translational modifications. Third, many transcripts give rise to more than one protein, through alternative splicing or alternative post-translational modifications. Fourth, many proteins form complexes with other proteins or RNA molecules, and only function in the presence of these other molecules.
One of the most promising developments to come from the study of human genes and proteins has been the identification of potential new drugs for the treatment of disease. This relies on genome and proteome information to identify proteins associated with a disease, which computer software can then use as targets for new drugs. For example, if a certain protein is implicated in a disease, its 3D structure provides the information to design drugs to interfere with the action of the protein. A molecule that fits the active site of an enzyme, but cannot be released by the enzyme, will inactivate the enzyme. This is the basis of new drug-discovery tools, which aim to find new drugs to inactivate proteins involved in disease. As genetic differences among individuals are found, researchers expect to use these techniques to develop personalized drugs that are more effective for the individual.
Understanding the proteome, the structure and function of each protein and the complexities of protein–protein interactions will be critical for developing the most effective diagnostic techniques and disease treatments in the future.
Without a clear understanding of concepts and methods of ‘molecular pathology’ and ‘proteomics’, one cannot follow my discussions of ‘scientific homeopathy. In this article I was trying to prepare the factual ground for understanding scientific discussions about homeopathy. Let us do that first. If any body ask why discuss all these things with homeopathy, I would say your question is like asking an engineer engaged in leveling of ground for constructing a house entrusted to him, that “you were entrusted to build my house, not to level the ground”. Without leveling the ground how can a house could be started constructing?
Proteins are macromolecules with complex structures and functions, and they act as the ‘molecular carriers of life process’. There is not a single biochemic reaction happening without the involvement of proteins in their capacities as enzymes, receptors, immune factors, structural factors and so on. First we have to understand ‘vital processes’ in terms of protein interactions. We have to understand the complex dynamics of ‘ligand-receptor’, ‘substrate-enzyme’ and ‘antigen-antibody’ interactions. Then we have to study the dynamics of ‘protein molecular inhibitions’, and the role of these inhibitions in the creation of pathological ‘molecular errors’. Only then we can understand the exact mechanism of how the pathogenic agents causes diseases. Then we can study therapeutics in terms of removal of these ‘molecular inhibitions’. Then I can explain the actual process involved in drug proving in terms of creating ‘molecular inhibitions’ caused by constituent molecules of our drug substances. Then we can understand ‘symptoms’ as expressions’ of ‘molecular errors’. Then my concept of drug potentization as ‘molecular imprinting’ and active principles of potentized drugs as ‘molecular imprints’ could be clearly understood. Then, i can explain how the ‘molecular imprints’ removes ‘protein inhibitions’ by their complementary configurational affinities to pathogenic molecules. That way we can understand the real molecular dynamics of homeopathic therapeutics involved in ‘similia similibus curentur’. Then you will understand my concepts of ‘miasms’ as ‘antibody mediated’ diseases caused by ‘off-target’ molecular inhibitions created by antibodies formed against exogenous’ proteins.
Modern drug designing technology, including computer aided drug designing, which is involved with designing of target specific drugs for rectifying molecular level pathologies, is an off-shoot of molecular medicine.
‘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’ 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.
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.
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 atoms 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.
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 occurring 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 imprints”.
According to modern scientific view, life exists through a series of inter-dependant and inter-connected complex chains of biochemical pathways, mediated by a highly organized and diversified class of organic bio-polymers known as proteins, which are considered to be ‘molecular carriers of life’.
Different types of proteins are synthesized according to the requirements from the building blocks known as amino acids, utilizing the genetic blueprint preserved in the DNA. Deficiency or malformation of protein molecules causes derangements in biochemical pathways. Nutritional deficiencies of building materials, errors in genetic blueprint or errors in various stages of genetic expressions may cause such deficiency or malformation of essential protein molecules, which are considered to be molecular errors underlying a broad class of ‘genetic diseases’ and ‘deficiency diseases’.
More over, exogenous or endogenous molecules or ions may bind to the essential protein molecules and lead to ‘molecular inhibitions’ of those proteins, thereby temporarily or permanently deactivating them. Such molecular inhibition and deactivation of essential protein molecules lead to the derangement of concerned biochemical pathways, leading to breakdown of vital processes, which amounts to a state of molecular level pathology. These exogenous and endogenous pathogenic molecules include environmental molecules, drugs, toxins, food articles, metabolic bye-products, infectious agents, antibodies or miasms and various such factors.
Primary basis of any state of pathology is some derangements occurring in the biochemical processes at the molecular level. Endogenous or exogenous foreign molecules or ions having any configurational similarity to certain biochemical ligands can mimic as original ones 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 pathological situations.
Homeopathy has devised its own method of closely following even the minutest deviations in the biochemical processes in the organism, through a special strategy of monitoring and recording the perceivable symptoms caused by such deviations. Obviously, derangement in a particular biochemical pathway resulting from such a nano-level molecular inhibition produces a specific train of subjective and objective symptoms in the organism. In other words, each specific group of symptoms exhibited by the organism indicates a particular error occurred in the molecular level. Homoeopathy chases these trains of symptoms to their minutest level, from periphery to interior, in order to study the exact molecular errors underlying any particular state of pathology. Not even the sophisticated tools of ultra-modern technologies can monitor those molecular errors with such perfection. Then, those pathological molecular inhibitions are removed by applying appropriate therapeutic agents, selected on the basis of ‘law of similars’ or ‘Similia Similibus Curentur’. This fundamental strategy underlying the homeopathic system of therapeutics evidently surpasses even the most scientific methods of modern molecular medicine. It is high time that the scientific world had realized and recognized this truth, and incorporated this wonderful tool into their armamentarium. Obviously, “similia similibus curentur” is the most effective technique of identifying and removing the pathological molecular inhibitions in the organism.
The subjective and objective symptoms presented by the organism are the only reliable indicators to help us correctly understand the minute molecular deviations underlying a state of pathology. Each group or trains of symptoms represent a specific molecular error that had occurred in a particular biochemical pathway. These symptoms invariably indicate the specific type and character of the endogenic or exogenic foreign molecules or ions responsible for the particular molecular inhibition. By studying the train of symptoms carefully and systematically, homoeopaths are really observing these exact molecular inhibitions. This symptomatology-based analytical method of homoeopathy is far more exact and superior to the multitude of expensive complex laboratory chemical tests and imaging technologies we consider to be scientific. Identifying the exact molecular errors in the organism of the patient by observing the expressed symptoms, and identifying the most appropriate therapeutic agents from the similarity of symptoms the drugs could produce in healthy organism- this is the scientific essence of “similia similibus curentur”.
If a drug substance in molecular form is introduced to a healthy living organism, which exists in state of comparatively dynamic equilibrium, constituent molecules of that drug substance are conveyed by the internal transport systems, and bind by their configurational affinity to any of the complex bio-molecules engaged in natural biochemical processes. As a result of such molecular binding, the bio-molecules are subjected to deviations in their three-dimensional configurations, and becomes incapacitated to deliver their natural molecular functions. All the biochemical processes mediated or participated by those bio-molecules are affected, and dependent biological pathways are subsequently blocked. Since different biological pathways are inter-depedent, deviations in one pathway naturally affects the dependent ones also. The cascading of molecular deviations influence the neuro mediator-neuro transmitter systems and endocrine systems and finally manifest in the form of particular groups of subjective and objective symptoms. This is the real molecular kinetics of pathology.
Homeopathy has devised its own peculiar way of experimenting and documenting the properties of medicinal substances in relation with their capability to produce various pathological conditions. This is called drug proving. For proving a particular drug substance, it is introduced into a healthy organism, and, the subjective and objective symptoms and their modalities representing the diverse molecular deviations caused by the drug, are carefully observed and recorded. Each specific group of symptoms that appear as part of diverse pathological conditions are thus artificially created in healthy individuals. These symptoms are compiled as a materia medica of the substance used.
Even though modern biochemistry and molecular medicine has made great strides in the study of diverse molecular inhibitions related with diseases, still there are grave limitations. It is imperative that modern science should strive to find out means to define the exact bio-molecular deviations and inhibitions responsible for each and every one of the multitude of diverse symptoms and modalities expressed in particular disease conditions, in order to evolve a most scientific method of removing such inhibitions. Homeopathy considers “totality of symptoms” as the only clue to the understanding of molecular level pathology, as well as deciding the appropriate therapeutic tools to rectify that molecular errors. Viewing from this perspective, “similia similibus curentur” is a highly scientific principle of therapeutics, deserving to be greatly honored by modern science at least in coming days.
Potentized homeopathic drugs contain ‘molecular imprints’ or ‘hydrosomes’, which can bind to the exogenous and endogenous pathogenic molecules having complementary affinity, thereby relieving the protein molecules from molecular inhibitions. This is the molecular mechanism of homeopathic therapeutics. ‘Hydrosomes’ or ‘Molecular Imprints’ are nanocavities formed in the ‘supra-molecular clusters of water and ethyl alcohol’, by a process of ‘molecular imprinting’ involved in potentization. When introduced into the organism, they act as artificial binding sites for pathogenic molecules having complementary configurational affinity, thereby relieving the biological molecules from pathological molecular inhibitions. This is the most rational and logical explanation of molecular dynamics of homeopathic therapeutics.
’Molecular imprints’ can be compared to ‘antibodies’. Antibodies are native proteins subjected to ‘molecular imprinting’ by ‘antigens’, and acting as binding sites for the specific antigens. ‘Molecular imprints’ in potentized drugs are supra-molecular clusters of water/alcohol, subjected to ‘molecular imprinting’ by constituent molecules of drug substances, and acting as artificial binding sites for pathogenic molecules having configurational similarity to drug molecules used for imprinting.
It is obvious that potentized drugs cannot rectify molecular errors arising from genetic errors and nutritional deficiencies. Scope of homeopathy is limited to the diseases originating from molecular inhibitions of proteins by exogenous or endogenous molecules. Homeopaths should remember these fundamental factors while discussing scope and limitations of homeopathy.
In scientific terms ‘similia similibus curentur’ means, “pathological molecular inhibitions underlying a disease and expressed through specific groups of subjective and objective symptoms can be removed by applying ‘molecular imprints’ of drug molecules, which in crude form could produce similar molecular inhibitions expressed through similar groups of symptoms”.
So far, we understood ‘Similia Similibus Curentur’ as ‘similarity of symptoms produced by drugs as well as diseases’. According to modern scientific understanding, we can explain it as ‘similarity of molecular errors produced by drug molecules and pathogenic molecules’ in the organism. To be more exact, that means ‘similarity of molecular configurations of pathogenic molecules and drug molecules’. Potentized drugs contains ‘molecular imprints’ of constituent molecules of drug used for potentization. ‘Molecular imprints’ are three-dimensional negatives of molecules, and hence they would have a peculiar affinity towards those molecules, due to their complementary configuration. ‘Molecular imprints’ would show this complementary affinity not only towards the molecules used for imprinting, but also towards all molecules that have configurations similar to those molecules. Homeopathy utilizes this phenomenon, and uses molecular imprints of drug molecules to bind and entrap pathogenic molecules having configurations similar to them. Similarity of configurations of drug molecules and pathogenic molecules are identified by evaluating the ‘similarity of symptoms’ they produce in organism during drug proving and disease. This realization is the the basis of scientific understanding of homeopathy I propose.
To be recognized as a scientific medical system, we should explain ‘Similia Similibus Curentur’ before the scientific community in a way fitting to the existing scientific paradigms, and should submit ourselves to be verified in accordance with scientific methods.
“Endogenous or exogenous pathogenic molecules that cause diseases by binding to the biological molecules can be entrapped and removed using molecular imprints of drug molecules which in molecular form can bind to the same biological molecules, utilizing the complementary configurational affinity between molecular imprints and pathogenic molecules”.
This scientific definition of ‘similia similibus curentur’ is the foundation of my claim that homeopathy is advanced branch of modern molecular medicine.
I do not think modern medicine is irrelevant or unscientific. Exactly, modern medicine has been advancing in parallel with human scientific knowledge. It plays main role in the health care system all over the world. Allopathy Hahnemann talks about is no more. It is not fair to call ‘modern medicine’ as allopathy. Modern medicine is ‘molecular medicine’, based on scientific understanding of vital processes. Remember this point when quoting ‘ant-allopathy’ statements of our masters.
Fundamental difference between homeopathy and modern medicine is that ‘modern medicine’ uses ‘drug molecules’ as therapeutic agents, where as homeopathy uses ‘molecular imprints’ of drug molecules. This is a very important difference, indeed.
Modern medicine has recently advanced into Molecular Medicine, where drugs are selected on the basis of scientific understanding of pathological molecular errors in vital processes.
Homeopathy selects drugs on the basis of ‘totality of symptoms’, which are the real indicators of those pathological molecular errors. As such, homeopathy can be defined as a specialized higher branch of ‘modern molecular medicine’.
Since ‘modern medicine’ uses highly reactive ‘drug molecules’ as therapeutic agents, they can create dangerous ‘off-target’ molecular errors in the organism. That is the main draw back of ‘modern medicine’. Since homeopathy uses only ‘molecular imprints’, they cannot cause any ‘off-target’ molecular errors. Hence homeopathy is very safe when compared to modern medicine.
Since ‘modern medicine’ requires a clear understanding of pathological molecular processes to decide an appropriate therapeutic agent, they cannot treat many diseases which are not well understood. For homeopathy, knowing the exact molecular error behind the pathology is not necessary, since homeopathy identifies the molecular errors and their remedial agents by observing subjective and objective ‘symptoms’ that express the molecular errors. As such, homeopathy can cure any disease even without knowing the underlying molecular errors, merely on the basis of ‘symptoms’. This is a great advantage for homeopathy. Whereas modern medicine can hope for an effective treatment only for well understood diseases, that to with possibility of unwanted side effects, homeopathy can treat any disease effectively and safely.
Existing more than 250 years as an independent therapeutic system totally alienated from mainstream scientific knowledge, I think time is now ripe for homeopathy to converges into modern molecular medicine, as an advanced branch of medical science. The great divide between ‘allopathy and homeopathy’ could now be effectively bridged through my scientific explanation of potentization and similia similibus curentur. Once the people belonging to molecular medicine realizes the historical implications of this convergence, I hope they would also utilize ‘molecular imprinting’ as part of their target-specific drug designing technology.