Chandran K C · @similimum
8th Jul 2015 from TwitLonger
#Medicine #Homeopathy #Potentization:
Homeopathic potencies are usually made using rectified spirit as the vehicle. But I am a bit suspicious about the appropriateness of this practice, since the protein molecules contained in the biological drugs would be denatured by the action of alcohol even before actual potentization happens. That means, the product we get will not be exact potencies of original drug molecules used for drug proving, but those of denatured molecules. This possibility will have serious implications on the therapeutic properties of such potentized drugs when applied on the basis of similia principle.
Now we have to learn something about protein structures and phenomenon of ‘denaturation’.
Proteins are amino acid polymers. A protein is created by ribosomes that “read” RNA that is encoded by codons in the gene and assemble the requisite amino acid combination from the genetic instruction, in a process known as translation. The newly created protein strand then undergoes post-translational modification, in which additional atoms or molecules are added, for example copper, zinc, or iron. Once this post-translational modification process has been completed, the protein begins to fold (sometimes spontaneously and sometimes with enzymatic assistance), curling up on itself so that hydrophobic elements of the protein are buried deep inside the structure and hydrophilic elements end up on the outside. The final shape of a protein determines how it interacts with its environment. The biological properties of proteins are due to their complex tertiary structure and three dimensional folding.
When a protein is denatured, the secondary and tertiary structures are altered but the peptide bonds of the primary structure between the amino acids are left intact. Since all structural levels of the protein determines its function, the protein can no longer perform its function once it has been denatured. This is in contrast to intrinsically unstructured proteins, which are unfolded in their native state, but still functionally active.
Denatured proteins can exhibit a wide range of characteristics, from loss of solubility to communal aggregation. Communal aggregation is the phenomenon of aggregation of the hydrophobic proteins to come closer and form the bonding between them, so as to reduce the total area exposed to water.
Ethyl alcohol, used as part of medium for potentization, is a very powerful ‘denaturing agent’ for protein molecules. Hence, protein molecules contained in the snake venoms and other products of biological origin undergo a process of ‘denaturation’ when added to alcohol-water mixture for potentization. It is these ‘denatured’ protein molecules that undergo ‘molecular imprinting’ during potentization.
This is applicable to all drug substances of protein nature, which would undergo denaturation at the initial stages of potentization, when added to water-ethyl alcohol medium. We have to remember this fact when discussing potentized drugs containing enzymes and other complex protein molecules.
This understanding also prompts us to search for other potential imprinting media that do not make molecular changes in proteins. We have to search for an ideal potentizing medium for biological drugs of protein nature- a medium that do not contain denaturing agents such as alcohol. I am thinking about water-glucose mixture for that purpose. Potentizing medium should not chemically interact with drug molecules, and they should not be harmful to human organism.
If pure water is used, the hydrogen bonding will be very temporary, and molecular imprints will not stand long. It will get dissociated. Presence of comparatively heavier molecules that can be part of supra-molecular networks of water is essential to make stable hydrogen bonding and molecular imprints.