Since CCRH has seriously undertaken drug proving as part of their research projects recently, I would like to bring some relevant points to the notice of researchers and authorities there.
Many drugs are proved in molecular forms (mother tinctures and potencies below Avogadro limit), whereas certain other drugs are proved in potencies above 12c.
My doubt is, whether the symptoms produced by same drug in high potencies and molecular forms will be similar? If they are different, how can we decide which symptoms are to be given more importance in the selection of similimum? I request the CCRH authorities to resolve this problem by conducting drug proving of same drug in both ways, and doing a comparative study of symptoms.
According to scientific view, ‘Similia Similibus Curentur’ means: ‘diseases caused by specific molecular inhibitions and expressed through specific groups of subjective and objective symptoms can be cured by potentized forms of drugs that could create similar pathologic molecular inhibitions and symptoms in healthy individuals if applied in crude form’. Same can be stated in a different way as: “pathological molecular inhibitions can be rectified using ‘molecular imprints’ of drug molecules that can create similar molecular inhibitions if applied in molecular form”.
Homeopathy utilizes ‘drug proving’ for studying the pathogenic properties of drug substances by observing their capacity to produce various pathological symptoms in healthy organisms. Homeopathy is based on the principle that a substance becomes a medicinal agent only because it has some disease-producing properties. In other words, if we could know what pathological inhibitions and symptoms a drug can create in healthy organism, we can decide in what disease states that drug could be used as a therapeutic agent in potentized form. Drug proving is unique to homeopathy. Whereas modern medicine studies the disease-curing properties of drugs, homeopathy studies the disease-producing properties of drugs. That makes a great difference.
Drug proving is done by administering small quantities of a particular drug to controlled volunteer groups of apparently healthy individuals. The subjective and objective symptoms, representing the diverse molecular deviations caused in the organism by the drug substance are carefully observed and recorded. These symptoms are systematically arranged compiled as materia medica of the substance used.
Let us examine what actually happens at molecular level during drug proving.
First point we have to note is that most drug substances, especially of vegetable or animal origin, are not ‘simple’ substance. Even if we use them as a ‘single’ substance, actually they consist of diverse types of individual molecules. A substance can interact with biological molecules only as individual molecules. If we really want to understand homeopathy and drug proving scientifically, we should first of all learn to perceive drug substance in terms of its diverse constituent molecules. Once we introduce a sample of drug substance into the living organism for ‘proving’, its constituent molecules are instantly subjected to various processes such as disintegration, ionization, hydration and certain chemical transformations.
Individual constituent molecules are carried and conveyed through blood and other internal transport systems into the cells and body fluids in different parts of the body. They can interact with various enzymes, receptors, and other biological molecules inside the organism. Individual drug molecules, in capacities of their molecular affinities, get themselves bound to various bio-molecules which participate in the essential biochemical activities in the organism. These interactions are decided and directed by the specific properties such as configurations and charges of active groups of individual drug molecules, and their specific affinity towards biological target molecules.
The three dimensional structure of the individual drug molecules, and that of the concerned bio-molecules are the decisive factors in this process of formation of molecular binding between them. This peculiarity is called molecular affinity. It is very important to note that drug substances interact with different biological molecules, not as a singular entity, but as individual constituent molecules and ions. These individual drug molecules and ions are capable of competing with natural ligands and substrates in binding to their biological targets, thereby inhibiting the essential bio-chemical processes which can take place only with their presence and mediation. Such molecular inhibitions in various bio-chemical pathways result in a condition of pathology, expressed in the form of a train of subjective and objective symptoms, due to the involvement of various neuro-mediator, neuro-transmitter and cellular signalling systems.
From this point of view, drug proving has to be done using molecular forms of drugs, since only they can produce real pathological molecular inhibitions in the organism.
To get this point clear, we have to differentiate between natural biochemical interactions and interactions of inhibitory nature.
Ligand- target Interactions such as those happening between ‘receptors and signaling molecules’’, ‘substrates and enzymes’ ‘antibodies and antigens’ etc can be considered typical biochemical interactions that are important for understanding molecular mechanism of homeopathic therapeutics.
A receptor is a molecule found on the surface of a cell, which receives specific chemical signals from neighboring cells or the wider environment within an organism. These signals tell a cell to do something—for example to divide or die, or to allow certain molecules to enter or exit the cell. In biochemistry, a receptor is a protein molecule, embedded in either the plasma membrane or the cytoplasm of a cell, to which one or more specific kinds of signaling molecules may attach. A molecule which binds (attaches) to a receptor is called a ligand, and may be a peptide (short protein) or other small molecule, such as a neurotransmitter, a hormone, a pharmaceutical drug, or a toxin. Each kind of receptor can bind only certain ligand shapes. Each cell typically has many receptors, of many different kinds. Simply put, a receptor functions as a keyhole that opens a neural path when the proper ligand is inserted.
Ligand binding stabilizes a certain receptor conformation (the three-dimensional shape of the receptor protein, with no change in sequence). This is often associated with gain of or loss of protein activity, ordinarily leading to some sort of cellular response. However, some ligands (e.g. antagonists) merely block receptors without inducing any response. Ligand-induced changes in receptors result in cellular changes which constitute the biological activity of the ligands. Many functions of the human body are regulated by these receptors responding uniquely to specific molecules like this.
Studies on the the shapes and actions of receptors have advanced the understanding of drug action at the binding sites of receptors.
Depending on their functions and ligands, several types of receptors may be identified:
1. Some receptor proteins are peripheral membrane proteins.
2. Many hormone and neurotransmitter receptors are transmembrane proteins: transmembrane receptors are embedded in the phospholipid bilayer of cell membranes, that allow the activation of signal transduction pathways in response to the activation by the binding molecule, or ligand.
3. Metabotropic receptors are coupled to G proteins and affect the cell indirectly through enzymes which control ion channels.
4. Ionotropic receptors (also known as ligand-gated ion channels) contain a central pore which opens in response to the binding of ligand.
5. Another major class of receptors are intracellular proteins such as those for steroid and intracrine peptide hormone receptors. These receptors often can enter the cell nucleus and modulate gene expression in response to the activation by the ligand.
One measure of how well a molecule fits a receptor is the binding affinity, which is inversely related to the dissociation constant. A good fit corresponds with high affinity and low dissociation constant. The final biological response (e.g. second messenger cascade, muscle contraction), is only achieved after a significant number of receptors are activated.
The receptor-ligand affinity is greater than enzyme-substrate affinity. Whilst both interactions are specific and reversible, there is no chemical modification of the ligand as seen with the substrate upon binding to its enzyme.
Many pathological molecular errors are caused by inhibitions of these receptors or enzymes by binding of exogenous or endogenous molecules or ions on them. Bacterial toxins, drugs and such pathological agents act this way.
When we prove our drugs in healthy people, the constituent molecules contained in the drug substances may bind to diverse types of ‘receptors’ or ‘enzymes’ due to the similarity of configurations between natural ligands and drug molecules. Molecules having ‘similar’ configuration can bind to similar receptors, causing similar pathological molecular errors expressed through ‘similar’ subjective and objective symptoms. The concept of ‘similarity of symptoms’ can be scientifically understood if we know the dynamics of ‘ligand-receptor’ and ‘substrate-enzyme’ relationships. Without this fundamental understanding one cannot follow the scientific explanations regarding ‘potentization’ and ‘similia similibus curentur’.
On the surface diverse enzyme molecules of characteristic three dimensional organizations, there will be different functional groups suitable for engaging in various types of biochemical bonds. Certain functional groups play a role in establishing contacts with other molecules, and are called ‘binding groups’. Functional groups performing real chemical processes are known as ‘active groups’. There are also ‘allosteric groups’ which facilitate interactions.
Different types of binding groups, active groups and allosteric groups exist on the same complex enzyme molecule. These binding sites, active sites and allosteric sites of bio-molecules interact with their substrates in a peculiar ‘key-lock’ mechanism, where the substrate acts as key. A key will be suitable only to the particular complimenting key- hole with exact three dimensional structure which fits to the shape of the key. In the same manner, various enzyme molecules engaged in biochemical processes identify and interact with their natural ligands or substrates with the help of peculiarities of their configurational and charge affinities.
Biochemical processes involves two aspects:
1.Binding of ligands to targets, which is determined by configurational affinity.
2. Chemical transformation, which is determined by charge affinity of ligands and targets.
Ligands with only configurational affinity to targets but no charge affinity, may bind to the target, but in the absence of charge affinity, no chemical transformations take place. This leads to molecular inhibitions of target molecules. This exactly like a fake key entering a key hole and failing to open the key and obstructing the lock. Molecular mechanism underlying pathological processes may be broadly compared to such an obstruction and inhibition of molecular locks by binding of some foreign molecules, partially similar to but different from original ones mimicking as the natural ligands. Due to such an inhibition, the particular enzymes or receptors become incapable of interacting with its natural molecular keys or ligands, thereby hindering the concerned normal biochemical process. This situation amounts to a pathology at molecular level. We can also visualize a different scenario of molecular inhibition, where the original key or ligand itself becoming structurally deformed, thereby hindering its interaction with its appropriate molecular lock. There may also be such occasions as some dirt getting collected inside the key-hole, or the key or the keyhole itself has some inherent manufacturing defects etc. All such presumed situations are possible in the case of bio-molecules also, and may result in bio-molecular inhibitions of some sort or other.
During drug proving, the constituent drug molecules interact with various biological molecules using this ‘key-lock’molecular mechanism, and create molecular inhibitions amounting to pathology. 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-dependant, deviations in one pathway naturally affects the dependent ones also. The cascading of molecular deviations influence the neuromediator-neurotransmitter systems and cellular signaling systems and finally manifest in the form of particular groups of subjective and objective symptoms. This is the real molecular kinetics of drug proving as well as pathology.
Based on this much of understanding regarding the molecular dynamics of pathology and drug action, let us examine the desirability of drug proving using potentized forms of drugs.
Drugs potentized above Avogadro limit never contain original drug molecules. They contain only ‘molecular imprints’ or ‘hydrosomes’ of individual constituent molecules. These molecular imprints can act only upon their original drug molecules, or pathological molecules having configurational similarity to those drug molecules. It is due to this complementary configurational affinity that potentized drugs act as therapeutic agents. Obviously, ‘molecular imprints’ contained in potentized drugs cannot as pathological agents. Then, how can we conduct drug proving using potentized drugs?
If drug molecules and pathogenic molecules are ‘molecular keys’ that can bind to specific biomolecular targets acing as ‘molecular locks’, molecular imprints contained in potentized drugs are ‘artificial key-holes’- not ‘duplicate keys’. Hence, olecular imprints can bind only to the ‘keys’ having configurational affinity.
Let us examine what actually happens when potentized drugs are administered into ‘apparently’ healthy individual individuals for drug proving. First point we need to remember is that ‘apparently’ healthy people will not be totally free from pathological molecular inhibitions. There will be diverse types of hidden molecular errors existing in them, arising from diverse types of factors such as nutritional, environmental, miasmatic, genetic, emotional, metabolic, infectious and others. When potentized drugs are introduced into the body, some or other molecular imprints contained in them may act upon these existing molecular inhibitions, which may be reflected as some transient symptoms. Actually, those symptoms are not indicating the ‘disease producing’ properties, but ‘diseases curing’ properties of concerned drugs. As such, symptoms obtained from drug proving using high potencies may confuse our materia medica.
Potentized drugs may act on ‘healthy’ organism by a different mechanism. Molecular imprints may bind to the natural ligands in the body, if they have any configurational affinity. But, such bindings will not lead to a state of pathology since molecular imprints cannot interfere in the interaction between natural ligands and targets which will have stronger affinity to each other. As such, symptoms appearing from such interactions will be very much temporary, and cannot be considered ‘pathological symptoms’
Based on the above observations, I request the CCRH authorities and scientists to conduct a comparative study of symptoms obtained from drug proving using potentized forms and molecular forms of same drugs.
I would like to mention another very important point in relation with this. Any study regarding high potency drugs should be done only using samples prepared under strict observations and supervision of researchers themselves. Never use commercially available samples, since a lot of malpractices are done in potentization. No commercially available ‘back potencies’ should also be used. Do the whole process of potentization starting from crude substance itself, to ensure we are using genuine samples for our research. Otherwise our whole work becomes unreliable.