spfpХранение и переработка сельхозсырьяStorage and Processing of Farm Products2072-96692658-767XРОСБИОТЕХ10.36107/spfp.2026.1.695spfp-695Research ArticleБИОТЕХНОЛОГИЧЕСКИЕ И МИКРОБИОЛОГИЧЕСКИЕ АСПЕКТЫBIOTECHNOLOGICAL AND MICROBIOLOGICAL ASPECTSМолекулярный докинг пептидов рапса с молекулами миелопероксидазы, дипептидилпептидазой IV и ангиотензин I-превращающим ферментомMolecular Docking of Rapeseed Peptides with Po, Dpp-iv and Ace Moleculeshttps://orcid.org/0000-0003-0847-0819МижеваАйслу АльбертовнаMizhevaAislu Albertovna

Аспирант 

Кафедра «Биотехнологии и биоорганического синтеза» ФГБОУ ВО Российский биотехнологический университет (РОСБИОТЕХ)

SPIN-код РИНЦ: 7120-7067

Graduate student 

Department of Biotechnology and Bioorganic Synthesis, Russian State Budgetary Educational Institution of Higher Education, Russian University of Biotechnology (ROSBIOTECH)

RSCI SPIN code: 7120-7067

mizheva.aislu@mail.ruhttps://orcid.org/0000-0003-2478-1705ФоменкоИван АндреевичFomenkoIvan Andreevich

Доцент кафедры «Биотехнологии и биоорганического синтеза» ФГБОУ ВО Российский биотехнологический университет (РОСБИОТЕХ)

SPIN-код РИНЦ: 5861-2838

Associate Professor of the Department of Biotechnology and Bioorganic Synthesis at the Russian Biotechnological University (ROSBIOTECH)

RSCI SPIN code: 5861-2838

iv.fomenko@mail.ruhttps://orcid.org/0000-0003-4298-0927ЧернухаИрина МихайловнаChernukhaIrina Mikhailovna

Главный научный сотрудник ФГБНУ «ФНЦ пищевых систем им. В.М. Горбатова» РАН, экспериментальная клиника – лаборатория биологически активных веществ животного происхождения, главный научный сотрудник ПНИЛ биотехнологии ФГБОУ ВО «Российский биотехнологический университет (РОСБИОТЕХ)»

SPIN-код: 3423-3754

Chief Researcher at the Russian Biotechnology University, V. M. Gorbatov Federal Research Center for Food Systems

imcher@inbox.ruhttps://orcid.org/0000-0002-3842-1391ДегтяревИван АлександровичDegtyarevIvan Aleksandrovich

Аспирант 

Кафедра «Биотехнологии и биоорганического синтеза» ФГБОУ ВО Российский биотехнологический университет (РОСБИОТЕХ)

SPIN-код РИНЦ: 9200-9527

Graduate student 

Department of Biotechnology and Bioorganic Synthesis, Russian State Budgetary Educational Institution of Higher Education, Russian University of Biotechnology (ROSBIOTECH)

RSCI SPIN code: 9200-9527

Ivand152@yandex.ruhttps://orcid.org/0000-0002-9287-0585МашенцеваНаталья ГеннадьевнаMashentsevaNatalya Gennadievna

Профессор кафедры «Биотехнологии и биоорганического синтеза» ФГБОУ ВО Российский биотехнологический университет (РОСБИОТЕХ)

SPIN-код РИНЦ: 9791-5806

Professor of the Department of Biotechnology and Bioorganic Synthesis at the Russian Biotechnological University (ROSBIOTECH)

RSCI SPIN code: 9791-5806

natali-mng@yandex.ruhttps://orcid.org/0009-0000-7677-6583АлексаночкинДенис ИгоревичAleksanochkinDenis Igorevich

Аспирант 

Кафедра «Биотехнологии и биоорганического синтеза» ФГБОУ ВО Российский биотехнологический университет (РОСБИОТЕХ)

SPIN-код РИНЦ: 1732-9580

Graduate student 

Department of Biotechnology and Bioorganic Synthesis, Russian State Budgetary Educational Institution of Higher Education, Russian University of Biotechnology (ROSBIOTECH)

RSCI SPIN code: 1732-9580

aleksanochkindi@list.ruРоссийский биотехнологический университетРоссияRussian Biotechnological UniversityRussian FederationРоссийский биотехнологический университет; Федеральный научно-исследовательский центр пищевых систем им. В. М. ГорбатоваРоссияRussian Biotechnological University, V. M. Gorbatov Federal Research Center of Food SystemsRussian Federation202617072026341695Copyright © Мижева А.А., Фоменко И.А., Чернуха И.М., Дегтярев И.А., Машенцева Н.Г., Алексаночкин Д.И., 20262026Мижева А.А., Фоменко И.А., Чернуха И.М., Дегтярев И.А., Машенцева Н.Г., Алексаночкин Д.И.Mizheva A.A., Fomenko I.A., Chernukha I.M., Degtyarev I.A., Mashentseva N.G., Aleksanochkin 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.spfp-mgupp.ru/jour/article/view/695Введение

Введение. Пептиды рапсового белка рассматриваются как перспективные биологически активные соединения, способные взаимодействовать с ферментативными мишенями, связанными с развитием сердечно-сосудистых и метаболических нарушений. В данной работе с использованием молекулярного докинга оценена комплементарность пептидов к активным центрам миеолопероксидазы, дипептидилпептидазы-IV и  ангиотензин I-превращающего фермента.

Цель

Цель. Установить in silico комплементарность пептидов гидролизата белков рапса активным центрам АПФ, ДПП-IV и МПО методом молекулярного докинга и отобрать наиболее перспективные последовательности для последующего химического синтеза и экспериментальной верификации.

Материалы и методы

Материалы и методы. Пептиды получены из ферментативного гидролизата белков рапса с использованием ферментного препарата «Alcalase 2.4 L FG». Пептидный профиль определяли методом ВЭЖХ-МС/МС. Определение потенциальной антиоксидантной и гипогликемической активности выполняли в БД «BIOPEP-UWM», антигипертензивного эффекта – в «AHTpin». Отобранные последовательности подвергали молекулярному докингу с миелопероксидазой, дипептидилпептидазой-IV и ангиотензин I-превращающим ферментом с использованием программ «AutoDock Vina» и «PyMOL». Анализ комплекса проводился по значениям энергии связывания и характеру взаимодействий с активными центрами мишеней в программе «Discovery Studio 2025 Client».   

Результаты

Результаты. Проведен скрининг пептидов гидролизата белка рапса с использованием молекулярного докинга с молекулами АПФ, ДПП-IV и МПО для дальнейшего химического синтеза. Наиболее отрицательные значения энергии связывания использовались как критерий отбора, что соответствует наиболее выгодному прогнозированию взаимодействию пептидов с целевыми мишенями. Наименьшие энергии связывания получены для комплексов YWDHNNPQIR-МПО (- 10,75±0,53 ккал/моль), YWDHNNPQIR-АПФ (- 9,54±0,47 ккал/моль) и DRNLRPF и ДПП-IV (- 8,36±0,41 ккал/моль).

Выводы

Выводы. Результаты докинга демонстрируют, что пептиды рапса способны образовывать прочные комплексы с молекулами АПФ, ДПП-IV и МПО и потенциально обуславливать антигипертензивные, антиоксидантные и гипогликемические свойства. Для последующего химического синтеза и экспериментальной верификации биологических свойств отобраны пептиды YWDHNNPQIR и DRNLRPF на основе наименьшей энергии связывания.  

Introduction

Introduction. Rapeseed protein peptides are considered promising biologically active compounds capable of interacting with enzymatic targets associated with the development of cardiovascular and metabolic disorders. In this study, molecular docking was used to evaluate the complementarity of the peptides to the active sites of myeloperoxidase, dipeptidyl peptidase-IV, and angiotensin I-converting enzyme.

Purpose

Purpose. Establish in silico the complementarity of rapeseed protein hydrolysate peptides to the active centers of ACE, DPP-IV, and MPO using molecular docking and to select the most promising sequences for subsequent chemical synthesis and experimental verification.

Materials and Methods

Materials and Methods. Peptides were obtained from rapeseed protein hydrolysate using the enzyme preparation Alcalase 2.4 L FG. Peptide profiling was performed using HPLC-MS/MS. Potential antioxidant and hypoglycemic activity were determined using the BIOPEP-UWM database, and the antihypertensive effect was assessed using the AHTpin database. The selected sequences were subjected to molecular docking with myeloperoxidase, dipeptidyl peptidase IV, and angiotensin I-converting enzyme using AutoDock Vina and PyMOL. The complex was analyzed based on binding energies and interaction patterns with the targets active sites using Discovery Studio 2025 Client.

Results

Results. Rapeseed protein hydrolysate peptides were screened using molecular docking with ACE, DPP-IV, and MPO molecules for further chemical synthesis. The most negative binding energies were used as the selection criterion, corresponding to the most favorable prediction of peptide interactions with the target molecules. The lowest binding energies were obtained for the YWDHNNPQIR-MPO complexes (-10.75±0.53 kcal/mol), YWDHNNPQIR-ACE (-9.54±0.47 kcal/mol), and DRNLRPF-DPP-IV (-8.36±0.41 kcal/mol).

Conclusion

Conclusion. Docking results demonstrate that rapeseed peptides can form strong complexes with ACE, DPP-IV, and MPO molecules and potentially exert antihypertensive, antioxidant, and hypoglycemic properties. Peptides YWDHNNPQIR and DRNLRPF were selected for subsequent chemical synthesis and experimental verification of their biological properties based on their lowest binding energies.

рапсовый белокбиоактивные пептидыin silico-скринингферментативный гидролизингибирование ферментовrapeseed proteinbioactive peptidesin silico screeningenzymatic hydrolysisenzyme inhibitionИсследование выполнено за счет гранта Российского научного фонда (проект № 25-16-00178). Соглашение № 25-16-00178 подписано 29.05.2025This work was performed under the Russian Science Foundation grant No. 25-16-00178ReferencesДегтярев, И. А., Гаравири, М., Фоменко, И. А., Вострикова, Н. Л., & Машенцева, Н. Г. (2025). Сравнение функционально-технологических свойств и аминокислотного состава изолятов белка растительного происхождения. Вестник Красноярского государственного аграрного университета, 2(215), 202–215. https://doi.org/10.36718/1819-4036-2025-2-202-215GOST 13496.4-2019. Feeds, compound feeds, and feed raw materials: Methods for determination of nitrogen and crude protein content. (In Russ.).Дегтярев, И. А., Фоменко, И. А., Чурмасова, Л. А., Мижева, А. А., & Машенцева, Н. Г. (2024). Способ получения комплекса полисахаридов из жмыха рапса с соэкстрагированным белком (Патент РФ № 2815687). Федеральная служба по интеллектуальной собственности.Degtyarev I. A., Mahmud G., Fomenko I. A., Vostrikova N. L., Mashentseva N. G. (2025). Comparison of functional and technological properties and amino acid composition of plant protein isolates. The Bulletin of KrasGAU, 2(215), 202–215. (In Russ.)Aluko, R. E. (2015). Antihypertensive peptides from food proteins. Annual Review of Food Science and Technology, 6(1), 235-262. https://doi.org/10.1146/annurev-food-022814-015520Degtyarev I. A., Fomenko I. A., Churmasova L. A., Mizheva A. A., Mashentseva N. G. (2024). Method for producing a polysaccharide complex from rapeseed meal with co-extracted protein. Russian Federation patent RU 2815687. (In Russ.).Aratani, Y. (2018). Myeloperoxidase: Its role for host defense, inflammation, and neutrophil function. Archives of Biochemistry and Biophysics, 640, 47-52. https://doi.org/10.1016/j.abb.2018.01.004General Pharmacopoeial Article OFS.1.2.3.0022.15. Determination of amine nitrogen by formol and iodometric titration methods. (In Russ.).Chai, T. T., Koh, J. A., Wong, C. C. C., Sabri, M. Z., & Wong, F. C. (2021). Computational screening for the anticancer potential of seed-derived antioxidant peptides: A cheminformatic approach. Molecules, 26(23), 7396. https://doi.org/10.3390/molecules26237396Aluko, R. E. (2015). Antihypertensive peptides from food proteins. Annual review of food science and technology, 6(1), 235-262.Chen, H. H., Li, W., Wang, Y., Xu, B., Hu, X., Li, X. B., & Xing, X. H. (2023). Mining and validation of novel hemp seed-derived DPP-IV-inhibiting peptides using a combination of multi-omics and molecular docking. Journal of Agricultural and Food Chemistry, 71(23), 9164-9174. https://doi.org/10.1021/acs.jafc.3c00535Aratani, Y. (2018). Myeloperoxidase: Its role for host defense, inflammation, and neutrophil function. Archives of biochemistry and biophysics, 640, 47-52.Cheng, C., Cui, H., Yu, X., & Li, W. (2025). Screening and Validation: AI-Aided Discovery of Dipeptidyl Peptidase-4 Inhibitory Peptides from Hydrolyzed Rice Proteins. Foods, 14(11), 1916. https://doi.org/10.3390/foods14111916Chai, T. T., Koh, J. A., Wong, C. C. C., Sabri, M. Z., & Wong, F. C. (2021). Computational screening for the anticancer potential of seed-derived antioxidant peptides: A cheminformatic approach. Molecules, 26(23), 7396.Chmielewska, A., Kozłowska, M., Rachwał, D., Wnukowski, P., Amarowicz, R., Nebesny, E., & Rosicka-Kaczmarek, J. (2021). Canola/rapeseed protein–nutritional value, functionality and food application: a review. Critical Reviews in Food Science and Nutrition, 61(22), 3836-3856. https://doi.org/10.1080/10408398.2020.1809342Chen, H. H., Li, W., Wang, Y., Xu, B., Hu, X., Li, X. B., & Xing, X. H. (2023). Mining and validation of novel hemp seed-derived DPP-IV-inhibiting peptides using a combination of multi-omics and molecular docking. Journal of Agricultural and Food Chemistry, 71(23), 9164-9174.Du, X., Li, Y., Xia, Y. L., Ai, S. M., Liang, J., Sang, P., Ji, X. & Liu, S. Q. (2016). Insights into protein–ligand interactions: mechanisms, models, and methods. International journal of molecular sciences, 17(2), 144. https://doi.org/10.3390/ijms17020144Cheng, C., Cui, H., Yu, X., & Li, W. (2025). Screening and Validation: AI-Aided Discovery of Dipeptidyl Peptidase-4 Inhibitory Peptides from Hydrolyzed Rice Proteins. Foods, 14(11), 1916.Duan, X., Dong, Y., Zhang, M., Li, Z., Bu, G., & Chen, F. (2023). Identification and molecular interactions of novel ACE inhibitory peptides from rapeseed protein. Food Chemistry, 422, 136085. https://doi.org/10.1016/j.foodchem.2023.136085Chmielewska, A., Kozłowska, M., Rachwał, D., Wnukowski, P., Amarowicz, R., Nebesny, E., & Rosicka-Kaczmarek, J. (2021). Canola/rapeseed protein–nutritional value, functionality and food application: a review. Critical Reviews in Food Science and Nutrition, 61(22), 3836-3856.Duan, X., Zhang, M., & Chen, F. (2021). Prediction and analysis of antimicrobial peptides from rapeseed protein using in silico approach. Journal of Food Biochemistry, 45(4), e13598. https://doi.org/10.1111/jfbc.13598Du, X., Li, Y., Xia, Y. L., Ai, S. M., Liang, J., Sang, P., ... & Liu, S. Q. (2016). Insights into protein–ligand interactions: mechanisms, models, and methods. International journal of molecular sciences, 17(2), 144.Elton, D. C., Boukouvalas, Z., Fuge, M. D., & Chung, P. W. (2019). Deep learning for molecular design – a review of the state of the art. Molecular Systems Design & Engineering, 4(4), 828-849. https://doi.org/10.1039/c9me00039aDuan, X., Dong, Y., Zhang, M., Li, Z., Bu, G., & Chen, F. (2023). Identification and molecular interactions of novel ACE inhibitory peptides from rapeseed protein. Food Chemistry, 422, 136085.Fadimu, G. J., Gan, C. Y., Olalere, O. A., Farahnaky, A., Gill, H., & Truong, T. (2023). Novel antihypertensive peptides from lupin protein hydrolysate: An in-silico identification and molecular docking studies. Food Chemistry, 407, 135082. https://doi.org/10.1016/j.foodchem.2022.135082Duan, X., Zhang, M., & Chen, F. (2021). Prediction and analysis of antimicrobial peptides from rapeseed protein using in silico approach. Journal of Food Biochemistry, 45(4), e13598.Fekete, M., Lehoczki, A., Kryczyk-Poprawa, A., Zábó, V., Varga, J. T., Bálint, M., Fazekas-Pongor, V., Csípő, T., Rząsa-Duran, E., & Varga, P. (2025). Functional foods in modern nutrition science: Mechanisms, evidence, and public health implications. Nutrients, 17(13), 2153. https://doi.org/10.3390/nu17132153Elton, D. C., Boukouvalas, Z., Fuge, M. D., & Chung, P. W. (2019). Deep learning for molecular design – a review of the state of the art. Molecular Systems Design & Engineering, 4(4), 828-849.Gao, J., Li, T., Chen, D., Gu, H., & Mao, X. (2021). Identification and molecular docking of antioxidant peptides from hemp seed protein hydrolysates. Lwt, 147, 111453. https://doi.org/10.1016/j.lwt.2021.111453Fadimu, G. J., Gan, C. Y., Olalere, O. A., Farahnaky, A., Gill, H., & Truong, T. (2023). Novel antihypertensive peptides from lupin protein hydrolysate: An in-silico identification and molecular docking studies. Food Chemistry, 407, 135082.Garbacz, K., Wawrzykowski, J., Czelej, M., & Waśko, A. (2025). In Silico Proteomic Profiling and Bioactive Peptide Potential of Rapeseed Meal. Foods, 14(14), 2451. https://doi.org/10.3390/foods14142451Gao, J., Li, T., Chen, D., Gu, H., & Mao, X. (2021). Identification and molecular docking of antioxidant peptides from hemp seed protein hydrolysates. Lwt, 147, 111453.Han, R., Maycock, J., Murray, B. S., & Boesch, C. (2018). Release of Angiotensin-Converting Enzyme (ACE) and Dipeptidyl Peptidase-IV (DPP-IV) inhibitory peptides from oilseed proteins – a bioinformatic prediction approach. Proceedings of the Nutrition Society, 77(OCE4), E230. https://doi.org/10.1017/S0029665118002367Garbacz, K., Wawrzykowski, J., Czelej, M., & Waśko, A. (2025). In Silico Proteomic Profiling and Bioactive Peptide Potential of Rapeseed Meal. Foods, 14(14), 2451.He, R., Alashi, A., Malomo, S. A., Girgih, A. T., Chao, D., Ju, X., & Aluko, R. E. (2013). Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates. Food Chemistry, 141(1), 153-159. https://doi.org/10.1016/j.foodchem.2013.02.087Han, R., Maycock, J., Murray, B. S., & Boesch, C. (2018). Release of Angiotensin-Converting Enzyme (ACE) and Dipeptidyl Peptidase-IV (DPP-IV) inhibitory peptides from oilseed proteins – a bioinformatic prediction approach. Proceedings of the Nutrition Society, 77(OCE4), E230.He, R., Yang, Y. J., Wang, Z., Xing, C. R., Yuan, J., Wang, L. F., Udenigwe, С. & Ju, X. R. (2019). Rapeseed protein-derived peptides, LY, RALP, and GHS, modulates key enzymes and intermediate products of renin–angiotensin system pathway in spontaneously hypertensive rat. NPJ science of food, 3(1), 1. https://doi.org/10.1038/s41538-018-0033-5He, R., Alashi, A., Malomo, S. A., Girgih, A. T., Chao, D., Ju, X., & Aluko, R. E. (2013). Antihypertensive and free radical scavenging properties of enzymatic rapeseed protein hydrolysates. Food Chemistry, 141(1), 153-159.Hossain, A., Rahman, M. E., Faruqe, M. O., Saif, A., Suhi, S., Zaman, R., Hirad, A. H., Matin, M. N., Rabbee, M. F. & Baek, K. H. (2024). Characterization of plant-derived natural inhibitors of dipeptidyl peptidase-4 as potential antidiabetic agents: a computational study. Pharmaceutics, 16(4), 483. https://doi.org/10.3390/pharmaceutics16040483He, R., Yang, Y. J., Wang, Z., Xing, C. R., Yuan, J., Wang, L. F., ... & Ju, X. R. (2019). Rapeseed protein-derived peptides, LY, RALP, and GHS, modulates key enzymes and intermediate products of renin–angiotensin system pathway in spontaneously hypertensive rat. NPJ science of food, 3(1), 1.Li, Y., Gao, X., Pan, D., Liu, Z., Xiao, C., Xiong, Y., Du, L., Cai, Z., Lu, W., Dang, Y. & Zhu, X. (2023). Identification and virtual screening of novel anti-inflammatory peptides from broccoli fermented by Lactobacillus strains. Frontiers in Nutrition, 9, 1118900. https://doi.org/10.3389/fnut.2022.1118900Hossain, A., Rahman, M. E., Faruqe, M. O., Saif, A., Suhi, S., Zaman, R., ... & Baek, K. H. (2024). Characterization of plant-derived natural inhibitors of dipeptidyl peptidase-4 as potential antidiabetic agents: a computational study. Pharmaceutics, 16(4), 483.Mao, M., Yu, X., Tian, G., Zhang, L., Huang, H., & Chu, Q. (2025). Discovery and functional validation of a novel lotus root-derived peptide (EWGHLGL) alleviating oxidative stress in vitro and in vivo. Food Chemistry, 493, 146013. https://doi.org/10.1016/j.foodchem.2025.146013Li, Y., Gao, X., Pan, D., Liu, Z., Xiao, C., Xiong, Y., ... & Zhu, X. (2023). Identification and virtual screening of novel anti-inflammatory peptides from broccoli fermented by Lactobacillus strains. Frontiers in Nutrition, 9, 1118900.Nong, N. T. P., & Hsu, J. L. (2022). Bioactive peptides: An understanding from current screening methodology. Processes, 10(6), 1114. https://doi.org/10.3390/pr10061114Nong, N. T. P., & Hsu, J. L. (2022). Bioactive peptides: An understanding from current screening methodology. Processes, 10(6), 1114.Purohit, K., Reddy, N., & Sunna, A. (2024). Exploring the potential of bioactive peptides: From natural sources to therapeutics. International Journal of Molecular Sciences, 25(3), 1391. https://doi.org/10.3390/ijms25031391Purohit, K., Reddy, N., & Sunna, A. (2024). Exploring the potential of bioactive peptides: From natural sources to therapeutics. International Journal of Molecular Sciences, 25(3), 1391.Saetang, J., Haewphet, T., Nilsuwan, K., & Benjakul, S. (2025). ACE-and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking. Biology, 14(5), 511. https://doi.org/10.3390/biology14050511Saetang, J., Haewphet, T., Nilsuwan, K., & Benjakul, S. (2025). ACE-and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking. Biology, 14(5), 511.Tang, X., Chen, X., Wang, H., Yang, J., Li, L., Zhu, J., & Liu, Y. (2023). Virtual screening technology for two novel peptides in soybean as inhibitors of α-amylase and α-glucosidase. Foods, 12(24), 4387. https://doi.org/10.3390/foods12244387Tang, X., Chen, X., Wang, H., Yang, J., Li, L., Zhu, J., & Liu, Y. (2023). Virtual screening technology for two novel peptides in soybean as inhibitors of α-amylase and α-glucosidase. Foods, 12(24), 4387.Thomas, M. K., Nikooienejad, A., Bray, R., Cui, X., Wilson, J., Duffin, K., Milicevic, Z., Haupt, A. & Robins, D. A. (2021). Dual GIP and GLP-1 receptor agonist tirzepatide improves beta-cell function and insulin sensitivity in type 2 diabetes. The Journal of Clinical Endocrinology & Metabolism, 106(2), 388-396. https://doi.org/10.1210/clinem/dgaa863Thomas, M. K., Nikooienejad, A., Bray, R., Cui, X., Wilson, J., Duffin, K., ... & Robins, D. A. (2021). Dual GIP and GLP-1 receptor agonist tirzepatide improves beta-cell function and insulin sensitivity in type 2 diabetes. The Journal of Clinical Endocrinology & Metabolism, 106(2), 388-396.Trott, O., & Olson, A. J. (2010). AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455–461. https://doi.org/10.1002/jcc.21334Wong, F. C., Xiao, J., Wang, S., Ee, K. Y., & Chai, T. T. (2020). Advances on the antioxidant peptides from edible plant sources. Trends in Food Science & Technology, 99, 44-57.Wei, K., Wan, Y., Wei, C., Liu, W., Wu, H., Leng, Y., Xu, M., Li, Y., Chen, Z., Wang, J., & Luo, H. (2025). Ultrasound-assisted preparation of antioxidant peptides in flaxseed meal: Purification, characterization and molecular docking analysis. Food Chemistry, 487, 144724. https://doi.org/10.1016/j.foodchem.2025.144724Xu, F., Yao, Y., Xu, X., Wang, M., Pan, M., Ji, S., ... & Wang, L. (2019). Identification and quantification of DPP-IV-inhibitory peptides from hydrolyzed-rapeseed-protein-derived napin with analysis of the interactions between key residues and protein domains. Journal of agricultural and food chemistry, 67(13), 3679-3690.Wong, F. C., Xiao, J., Wang, S., Ee, K. Y., & Chai, T. T. (2020). Advances on the antioxidant peptides from edible plant sources. Trends in Food Science & Technology, 99, 44-57. https://doi.org/10.1016/j.tifs.2020.02.012Zhu, D., Zheng, H., Xiaolin, X., & Zhang, B. (2025). A Novel Antioxidant Peptide from Black Soybean (Glycine max (L.) Merr.) with Verified MPO Interaction and Multi-Scale Antioxidant Activity. Frontiers in Nutrition, 12, 1649684.Xu, F., Yao, Y., Xu, X., Wang, M., Pan, M., Ji, S., ... & Wang, L. (2019). Identification and quantification of DPP-IV-inhibitory peptides from hydrolyzed-rapeseed-protein-derived napin with analysis of the interactions between key residues and protein domains. Journal of agricultural and food chemistry, 67(13), 3679-3690. https://doi.org/10.1021/acs.jafc.9b01069Xu, F., Yao, Y., Xu, X., Wang, M., Pan, M., Ji, S., ... & Wang, L. (2019). Identification and quantification of DPP-IV-inhibitory peptides from hydrolyzed-rapeseed-protein-derived napin with analysis of the interactions between key residues and protein domains. Journal of agricultural and food chemistry, 67(13), 3679-3690. https://doi.org/10.1021/acs.jafc.9b01069Zhu, D., Zheng, H., Xiaolin, X., & Zhang, B. (2025). A Novel Antioxidant Peptide from Black Soybean (Glycine max (L.) Merr.) with Verified MPO Interaction and Multi-Scale Antioxidant Activity. Frontiers in Nutrition, 12, 1649684. https://doi.org/10.3389/fnut.2025.1649684Zhu, D., Zheng, H., Xiaolin, X., & Zhang, B. (2025). A Novel Antioxidant Peptide from Black Soybean (Glycine max (L.) Merr.) with Verified MPO Interaction and Multi-Scale Antioxidant Activity. Frontiers in Nutrition, 12, 1649684. https://doi.org/10.3389/fnut.2025.1649684

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