Scheme of chemical bonding between basic and hydrolyzed forms of amide and carboxyl forms of nitrile glycosides under various conditions in vivo around and in cancer cell

article - DOI: 10.2174/1871520620999201103201008
monograph - DOI: 10.5281/zenodo.7295357 | ISBN: 978-619-91534-4-4
ATLAS - presentation of the finale information in the most applied and convenient form of application - DOI: 10.5281/zenodo.8009390 | ISBN: 978-619-91534-5-1

...The compound thus obtained exhibits hydrolytic inertness at pH=6.4. Thus, the resulting form HF(A;C) reaches unaltered to the cell membrane of the cancer cell. These compounds are due to the sharing of incomplete electron charges and are stabilized by a solvate shell of water. The shortage of OH groups further stabilizes the process, due to the slightly acidic medium and free protons oriented directly above the cell membrane. In parallel with this process, reverse hydrolysis takes place from HF(C) to BF(C) - which retains activity and leaves the associated volume around the cancer cell, re-hydrolyzes and binds a new amount of HF(A) and enters into the closed volume.

The HF(A) molecule contains at least one glycosidic group. The compound is saturated with ammonia (-NH₃⁺) and readily binds with protein to glycoprotein. The hydrolysis-modified form is passed through a protein carrier through the cell membrane. Here, however, pH is equal to 7.4 and saturation of OH groups. Thus, HF(B) is obtained, i.e. there is a partial shift of the hydrolytic equilibrium from HF(A) through BF(A) to HF(B). An enzyme amidase is also synthesized in the cell, which converts -(CO).NH₂ to -(COOH). As a final product under these conditions we have all three hydrolytic forms - HF(A;B;C).

Therefore, the eventual chemical apoptosis will proceed independently of all enzymes synthesized according to instructions from cancer DNA (for example, the linamarase gene to linamarase)...