vguitВестник Воронежского государственного университета инженерных технологийProceedings of the Voronezh State University of Engineering Technologies2226-910X2310-1202VSUET10.20914/2310-1202-2026-3-239-252vguit-3903Research ArticleПищевые системыFood systemsОценка биологической активности пептидов конопли, полученных с использованием растительных ферментовAssessment of the Biological Activity of Hemp Peptides Produced Using Plant-Derived Enzymeshttps://orcid.org/0009-0000-7677-6583АлексаночкинД. И.AleksanochkinD. I.aleksanochkindi@list.ruhttps://orcid.org/0000-0003-2478-1705ФоменкоИ. А.FomenkoI. A.iv.fomenko@mail.ruhttps://orcid.org/0000-0002-9287-0585МашенцеваН. Г.MashentsevaN. G.natali-mng@ya.ruhttps://orcid.org/0009-0002-1213-0729МухтаровД. И.MukhtarovD. I.muhtarovdaniil87@gmail.comРоссийский биотехнологический университетРоссияRussian Biotechnological UniversityRussian Federation202601102026883239252Copyright © Алексаночкин Д.И., Фоменко И.А., Машенцева Н.Г., Мухтаров Д.И., 20262026Алексаночкин Д.И., Фоменко И.А., Машенцева Н.Г., Мухтаров Д.И.Aleksanochkin D.I., Fomenko I.A., Mashentseva N.G., Mukhtarov D.I.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.vestnik-vsuet.ru/vguit/article/view/3903

В работе проведено комплексное исследование биологически активных пептидов, полученных при ферментативном гидролизе белка промышленной конопли протеазами растительного происхождения (бромелаином и папаином). Целью исследования являлась идентификация пептидных последовательностей и оценка их потенциальной биологической активности методом молекулярного докинга. С использованием ВЭЖХ LC-MS/MS были идентифицированы 2381 и 2752 пептидов в гидролизатах белка конопли, обработанных бромелаином и папаином, соответственно. Прогнозирование с помощью базы данных BIOPEP-UWM показало, что все полученные последовательности обладают ингибирующей активностью в отношении АПФ и ДПП4. Также некоторые пептиды ингибировали ренин, α-глюкозидазу, глутаматкарбоксипептидазу II и неприлизин, дополнительно были выявлены антиоксидантные, иммуностимулирующие и нейропротекторные свойства. In silico оценка физико-химических параметров подтвердила высокую растворимость, отсутствие токсичности и умеренную стабильность в условиях, имитирующих кишечную среду и кровь: средний период полураспада пептидов в кишечнике, полученных с использованием бромелаина, составлял 1,2 с, а у папаиновых последовательностей – 1,25 с; средний период полураспада в крови составил 13,6 мин для всех пептидов. Результаты молекулярного докинга в AutoDock Vina выявили высокую ингибирующую способность пептидов к активным центрам белков-мишеней (с энергией связывания от -5,749 до -11,120 ккал/моль). В качестве пептидов с наименьшей энергией взаимодействия были выбраны: YGRDEISVF с АПФ (-9,569 ккал/моль); FDERIRE с ДПП4 (-7,995); NPHEDFPQSRR c МПО (-11,120); ARFDERIRE c ренином (-7,728); GNPEDEFEQLRR с альфа-глюкозидазой (-6,535); YGRDEISVF с GCP2 (-9,702); AREPDTRVE с неприлизином (-9,333). Была выявлена зависимость между величиной энергии связывания и количеством контактов с ключевыми карманами (активными центрами) белков-мишеней. Полученные данные указывают на перспективность пептидов конопли как биоактивных агентов. Выбранный нами подход позволяет выбрать пептиды, которые в дальнейшем будут исследоваться in vitro и in vivo.

A comprehensive study of biologically active peptides obtained by enzymatic hydrolysis of industrial hemp protein by proteases of plant origin (bromelain and papain) has been carried out. The aim of the study was to identify peptide sequences and evaluate their potential biological activity by molecular docking. Using LC-MS/MS HPLC, 2381 and 2752 peptides were identified in hemp protein hydrolysates treated with bromelain and papain, respectively. Prediction using the BIOPEP-UWM database showed that all the obtained sequences have inhibitory activity against ACE and DPP4. Also, some peptides inhibited renin, α-glucosidase, glutamate carboxypeptidase II and neprilysin, additionally antioxidant, immunostimulating and neuroprotective properties were revealed. In silico, the evaluation of physico-chemical parameters confirmed high solubility, no toxicity, and moderate stability under conditions simulating the intestinal environment. The average half–life of peptides in the intestine obtained using bromelain was 1.2 s, and that of papain sequences was 1.25 s. The average blood half-life was 13.6 minutes for all peptides. The results of molecular docking in AutoDock Vina revealed a high inhibitory ability of peptides to the active sites of target proteins (with binding energies from -5.749 to -11.120 kcal/mol). The following peptides with the lowest interaction energy were selected: YGRDEISVF with ACE (-9.569 kcal/mol); FDERIRE with DPP4 (-7.995); NPHEDFPQSRR with MPO (-11.120); ARFDERIRE with renin (-7.728); GNPEDEFEQLRR with alpha-glucosidase (-6.535); YGRDEISVF with GCP2 (-9.702); AREPDTRVE with non-lysine (-9.333). A relationship was revealed between the amount of binding energy and the number of contacts with key pockets of target proteins. The data obtained indicate the prospects of cannabis peptides as bioactive agents. The approach we have chosen allows us to select peptides that will be further studied in vitro and in vivo.

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The authors declare that there are no conflicts of interest present.