[Possibility of biocompatibility of fullerene C60 with oligopeptides using a comparative analysis of their spatial form].
It was proposed to elucidate the mechanism of unique biological biocompatibility of carbon materials used for making endoprostheses for medicinal practice. For this purpose, a method of comparing the geometry of individual globular and fibrillar proteins and carbon structures (fullerenes) was advanced, and a comparative analysis of the spatial structure of fullerene C60 and the amino acid sequences of 286 proteins was made. Based on a high degree of similarity in the positions of atoms of the polypeptide chains of proteins and peptides and the corresponding atoms of fullerene and of other structural parameters revealed by the comparison of the spatial structures using mathematical simulation, the phenomenon of biological compatibility was interpreted as an "insertion" of fullerenes into the structure of protein molecules in place of structurally similar amino acid sequences, i.e., as a "prosthetics" at the molecular level. It is proposed that fullerenes can "simulate" structurally similar short peptides in biological processes. It was shown that noncarbon biogenic atoms play a large role in the formation of specific structure of protein molecules.
Baranov
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AA
NIIGRAFIT State Research Institute of Graphite-Based Structural Materials, Moscow, Russia.
Esipova
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NG
D000595:Amino Acid Sequence; D002244:Carbon / Q000737:chemistry*; D037741:Fullerenes; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*
D037741:Fullerenes; D009842:Oligopeptides; D002244:Carbon; C069837:fullerene C60