Food Processing: Techniques and Technology Food Processing: Techniques and Technology Техника и технология пищевых производств 2074-9414 2313-1748 92564 10.21603/2074-9414-2024-4-2536 ОРИГИНАЛЬНАЯ СТАТЬЯ ORIGINAL ARTICLE ОРИГИНАЛЬНАЯ СТАТЬЯ Amino Acid Patterns that Determine Antihyperuricemic Activity of Peptides: Identification and Predictive Analysis Идентификация и предиктивный анализ аминокислотных паттернов, обуславливающих потенциальную антигиперурикемическую активность пептидов Смирнова Анастасия Вадимовна Smirnova Anastasia V. https://orcid.org/0000-0003-4863-9834 Тихонов Сергей Леонидович Tikhonov Sergey L. tihonov75@bk.ru Уральский государственный экономический университет Екатеринбург Россия Ural State University of Economics Yekaterinburg Russian Federation Фонд поддержки проектов Национальной технологической инициативы Москва Россия National Technology Initiative Project Support Fund Moscow Russian Federation Уральский государственный экономический университет Екатеринбург Россия Ural State University of Economics Yekaterinburg Russian Federation Уральский государственный лесотехнический университет Yekaterinburg RU Ural State Forestry Engineering University Yekaterinburg RU 24 12 2024 24 12 2024 54 4 687 700 15 01 2024 05 03 2024 https://fptt.ru/en/issues/23109/23123/

Пептиды являются потенциально перспективными аналогами синтетических лекарственных препаратов для лечения гиперурикемии. Цель исследования – идентифицировать устойчивые аминокислотные паттерны, обуславливающие ингибирующую ксантиноксидазную активность пептидов, предложить на их основе новые антигиперурикемические пептиды с доказанной посредством использования методологии пред иктивной аналитики in silico эффективностью. Объектами исследования являлись пептиды, обладающие ингибирующей ксантиноксидазной активностью. В работе применялась авторская программа поиска, идентификации и количественной оценки повторяющихся сочетаний аминокислотных остатков в целевых пептидных последовательностях. Проводили оценку физико-химических и фармакокинетических свойств, ингибирующей ксантиноксидазной активности, общей и целевой биологической активности, а также токсичности идентифицированных пептидов. Количество аминокислот в цепи, изоэлектрическая точка, заряд при нейтральном pH, молекулярная масса пептидов и индекс гидрофобности были рассчитаны теоретически. Идентифицированы аминокислотные паттерны, ответственные за процесс ингибирования фермента ксантиноксидазы, сгенерированы новые пептидные последовательности. Идентифицированы 49 нетоксичных пептидов с различной длиной аминокислотной последовательности, обладающих потенциально высокой антимикробной и ингибирующей активностью в отношении целевых мишеней лекарственных препаратов, используемых при гиперурикемии и сахарном диабете 2 типа. Пептиды охарактеризовали как низкомолекулярные соединения гидрофильной (преимущественно) и гидрофобной природы длиной от 4 до 7 аминокислот, содержащие в структуре преимущественно аминокислотные остатки пролина, триптофана и фенилаланина со средней молекулярной массой 723 Да и отрицательным зарядом. Результаты данного исследования являются важным шагом в понимании молекулярных механизмов ингибирования фермента ксантиноксидазы и открывают новые перспективы для разработки антигиперурикемических пептидных препаратов.

Peptides offer a promising analogue to synthetic drugs in treating hyperuricemia. This article introduces reliable amino acid patterns that cause the inhibitory xanthine oxidase (CSR) activity of peptides. The research objective was to propose new antihyperuricemic peptides and prove their effectiveness by predictive analytics in silico. The study featured peptides with inhibitory xanthine oxidase activity. The authors developed a protocol for searching, identifying, and quantifying patterns of amino acid residues in target peptide sequences. The identified peptides were tested for physicochemical properties, pharmacokinetic profile, inhibitory xanthine oxidase activity, general and target biological activity, and toxicity. The research revealed amino acid patterns responsible for inhibiting the xanthine oxidase enzyme, as well as generated new peptide sequences. Forty-nine non-toxic peptides with different lengths of amino acid sequences demonstrated high antimicrobial and inhibitory potential against the targeted drugs used to treat hyperuricemia and type 2 diabetes mellitus. The peptides were low-molecular compounds of predominantly hydrophilic and hydrophobic nature, 4-7 amino acids long. They contained negatively charged amino acid residues of proline, tryptophan, and phenylalanine with an average molecular weight of 723 Da. The study offers an important insight into the molecular mechanisms of xanthine oxidase inhibition and opens up new prospects for developing novel antihyperuricemic peptide drugs.

 Пептиды гиперурикемия ингибиторы ксантиноксидазы аминокислотные паттерны IC50 Peptides hyperuricemia xanthine oxidase inhibitors amino acid patterns IC50

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