Russian Journal of Biological Physics and Chemisrty Russian Journal of Biological Physics and Chemisrty АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ 2499-9962 54491 Общая биофизика General biophysics Общая биофизика Biologically active fragments of protein structures of global proteome Биологически активные фрагменты белковых структур глобального протеома Замятнин А А Zamyatnin A A aaz@inbi.ras.ru Белозерская Т А Belozerskaya T A Институт биохимии им. А.Н. Баха, ФИЦ «Фундаментальные основы биотехнологии» РАН ru A.N. Bach Institute of Biochemistry, Research Centre of Biotechnology Russian Academy of Sciences ru Институт биохимии им. А.Н. Баха, ФИЦ «Фундаментальные основы биотехнологии» РАН ru A.N. Bach Institute of Biochemistry, Research Centre of Biotechnology Russian Academy of Sciences ru 25 03 2020 25 03 2020 5 1 69 80 20 03 2020 20 03 2020 https://rusjbpc.ru/en/nauka/article/54491/view

В основе гигантского биоразнообразия лежит также гигантское, молекулярное разнообразие линейных комбинаций 20 аминокислотных остатков в пептидных структурах. Их совокупность представляет собой глобальный протеом Земли. Расшифрованы аминокислотные последовательности ~200 миллионов природных пептидных структур. Полагается, что каждая из них предназначена для выполнения определенной роли в живом организме. Несмотря на столь значительное число известных пептидных молекул, бóльшая часть глобального протеома еще не расшифрована. Тем не менее, известная информация уже используется для различных анализов и обобщений. Огромная часть подобных анализов посвящена изучению фрагментов представителей глобального протеома. Теоретически возможное число разных пептидных структур, составленных всего лишь из 50 аминокислотных остатков, характеризуется величиной ~1034. Огромное число фрагментов таких структур послужило основанием для возникновения понятия фрагментомики - направления, в рамках которого исследуется структура и функции совокупности белковых фрагментов. Эти данные в течение 30 лет собираются и изучаются в базе данных EROP-Moscow, и их число составляет более 26000. Среди них большое количество регуляторов нервной, эндокринной и иммунной систем, а также разнообразные антимикробные олигопептиды, ингибиторы ферментов и многие другие, обладающие специфическими физико-химическими особенностями. Анализ информации базы данных EROP-Moscow позволил сделать вывод о том, что регуляторные олигопептиды возникают из трех источников. Это - олигопептидные регуляторы, выщепляемые из эндогенных специализированных предшественников с помощью особых ферментов, обычные эндогенные белки-полипептиды (например, гемоглобин, альбумин и т.д.), расщепляемые протеолитическими ферментами до небольших фрагментов, а также экзогенные белки или их фрагменты, поступающие в организм извне в результате приема пищи или укуса (например, насекомых). Они в организме формируют постоянно меняющийся пул эндогенных и экзогенных веществ пептидной природы (континуум), включенный в функционирование всех регуляторных систем.

Giant biodiversity is based on the gigantic molecular diversity of linear combinations of 20 amino acid residues in peptide structures. Their combination is a global proteome of the Earth. The amino acid sequences of ~200 million natural peptide structures have been decoded. It is believed that each of them is dedicated a specific role in a living organism. Despite such a significant number of known peptide molecules, a good part of the global proteome has not yet been deciphered. However, familiar information is already used for various analyses and generalizations. A large part of such analyses is devoted to the study of fragments representing the global proteome. Theoretically, the possible number of different peptide structures composed of only 50 amino acid residues is characterized by a value of ~1034. A huge number of such structure fragments served as the basis for the emergence of the concept of fragmentomics - a direction which studied the structure and functions of a set of protein fragments. These data have been collected and studied in the EROP-Moscow database for 30 years, and their number is more than 26,000 now. A large number of regulators of the nervous, endocrine and immune systems, as well as a variety of antimicrobial oligopeptides, enzyme inhibitors, and many others possessing specific physical and chemical features were among them. The analysis of the EROP-Moscow database information allowed us to conclude that regulatory oligopeptides arise from three sources. These are oligopeptide regulators cleaved from specialized endogenous precursors using special enzymes, ordinary endogenous protein polypeptides (for example, hemoglobin, albumin, etc.), cleaved by proteolytic enzymes to small fragments, as well as exogenous proteins or their fragments entering the body from the outside as a result of a meal or bite (e.g., insects They form in the organism a constantly changing pool of endogenous and exogenous substances of peptide nature (continuum), which is included in the functioning of all regulatory systems.

 протеом белковые структуры proteome protein structures

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