Copyright © 2000, 2001, 2002, 2006 by Galen Daryl Knight and VitaleTherapeutics, Inc.

VITALETHINE AND BETA-ALETHINE:
AUTHENTIC MASS SPECTRA vs. ARTIFACTS

The mass spectra of authentic vitalethine produces slightly higher mass ions [in boxes] than expected (under boxes), probably because it was taken from deuterated water and some of its hydrogens (on the nitrogens and on the carbamic/carbonimidic portions of the molecule) probably exchanged with the [heavier deuterium]. The mass ion, for example for vitalethine is observed at 384 and 406 (Na+ adduct) instead of 383.466 and 405.448, the small peaks for masses also being broad instead of sharp because of these isotopic effects.



Although there is some evidence for decomposition to beta-aletheine (isotopic = 149.075, average = 149.235), or at least formation of a doubly charged beta-alethine (148.2275, average) that has exchanged some deuterium for hydrogen, intensities for these masses are generally much less than those observed for beta-alethine's masses (Average = 296.455 for the H+ adduct and 317.429 for the Na + adduct) in the authentic preparations of both vitalethine and beta-alethine.

These amplitudes contrast sharply with the peak intensities for masses in others' attempts to make the authentic compounds. The bromo (372.9) and bis-Schiff base (188.2) derivatives, whose structures are identified below, yield almost as much intensity in their mass spectra of these contaminated preparations as the disulfide, beta-alethine, does at 295.1. Thus, these derivatives appear to be artifacts produced by serious departures from the authentic procedures for making both authentic vitalethine and beta-alethine. These contaminants, in others' preparations identified below, are alarming, since they probably constitute analogues and therefore competitive inhibitors of the vitalethine produced naturally by our bodies. Thus, these artifacts produced by others can conceivably poison all the important functions of vitalethine in the body, including vitalethine's stimulation of immune surveillance for cancer cells.

Such contaminated preparations of beta-alethine also seem to be particularly unstable, decomposition to the monomer at 148.4 appearing in the contaminated preparations as a peak more than twice the % amplitude observed for the desired authentic dimer's peak. Crudely estimating, then, the masses for the expected adducts with beta-alethine's authentic dimer constitutes about four fifths (80%) of the peak intensities, whereas the contaminated preparation has only about one fifth (20%) of its peak intensities in those representing anything even close to the mass ions expected for beta-alethine. The logical explanation for this is that the contaminating brominated derivative, bromine bound to the amide nitrogen, makes their contaminated preparations more likely to decompose into either the monomer or its mixed disulfide with cysteamine, depending upon which way bromine enhances the hydrolysis or cleavage. Both of these artifactual decomposition products are in much greater abundance in others' contaminated preparations of beta-alethine than in any of the authentic preparations of beta-alethine and vitalethine prepared by the "true Inventors". Note that there is no evidence for an artifactual mass at 188.2 in either authentic vitaletheine or authentic beta-alethine, nor is there an artifactual mass at 372.9 in either pure authentic preparation.

The preparations contaminated with the brominated, bis-acetone Schiff bases, and with mixed disulfides with cysteamine, present issues of authenticity, stability, and safety. These contaminated preparations are reportedly tens of thousands of times less potent than authentic beta-alethine in biological assays, possibly confirming suspicions that the biological activity of authentic beta-alethine results from traces of vitalethine (masses observed at 433, 473, 530) formed by equilibration of beta-alethine with atmospheric carbon dioxide, just as carbamino adducts are known to form with the amino groups in hemoglobulin (respiration) and in the protein in plants involved in trapping CO2 for photosynthesis. The bis-acetone Schiff bases on beta-alethine artifactually prevent this CO2/carbamate equilibration from occurring, and because of the structural similarity of this artifact to vitalethine, these contaminants probably also competitively inhibit the biological activities of vitalethine. Hence, the dramatic drop in potency and stability of beta-alethine when others fail to completely removing bromide ions and through their failure to use the right solvent, both failures being devastating departures from the authentic synthetic procedure that uses acetonitrile instead of the problematic acetone.

Logically, then, the Schiff bases with contaminating acetone preclude the formation of most (if not all) stable vitalethine by blocking the free amino groups of beta-alethine needed to react with carbon dioxide or with phosgene to form vitalethine, through natural equilibration or in the authentic synthetic procedure, respectively. The contaminating bromide ions also tend to prevent the formation of vitalethine by helping to disproportionate the desirable disulfide into the thiol or reduced form of vitalethine, the thiol form being very difficult to synthesize, chemically, probably because of the tendency of the thiol to attack the amide intramolecularly, and the tendency of the resulting amino-ortho ester to then attack the carbamic/carbonimidic ends of vitalethine, thereby altering the terminal carbamic/carbonimidic functional group that makes vitalethine about a trillion times more potent than beta-alethine.

Note that the polymerized or higher aggregate masses observed in vitalethine, only traces of which were also found in beta-alethine, only appear in the MALDI mass spectrometer, and that these probably result from polymerization, or at least complexation reactions caused by the UV laser in the mass spectrometer. These reactions are no doubt similar to 1) those UV-polymerizing reactions already proposed for these types of compounds in the ortho-ester-like synthesis of authentic vitaletheine V4 (the tetramer), and to 2) the ortho-ester-like, highly therapeutic sulfenate-linked benzyl carbamate dimer. The proton and carbon NMR for the authentic preparations of beta-alethine and for authentic vitalethine confirm this conclusion, since these authentic preparations appear to be pure, with little (if any) NMR evidence for the heterogeneity and decompositions observed in the MALDI mass spectrometer.

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