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Discovery and molecular mechanism of a novel antihypertensive peptide from Chlamydomonas reinhardtii based on molecular docking, molecular dynamics simulation, in vitro, and in vivo analysis

文献类型：期刊论文

作者Suo, Qishan1,2,3; Yue, Yang1,2; Wang, Jing1,2; Wu, Ning1,2; Geng, Lihua1,2; Zhang, Quanbin1,2,3
刊名FOOD RESEARCH INTERNATIONAL
出版日期2026-04-01
卷号229页码:13
关键词Chlamydomonas reinhardtii peptides Angiotensin converting enzyme inhibitor Molecular dynamics simulation Virtual screening Antihypertensive functional food
ISSN号0963-9969
DOI10.1016/j.foodres.2026.118477
通讯作者Yue, Yang(yueyang@qdio.ac.cn) ; Zhang, Quanbin(qbzhang@qdio.ac.cn)
英文摘要Chlamydomonas reinhardtii, a nutrient-rich microalga and emerging food resource, remains largely unexplored as a source of bioactive peptides. In this study, eight protease hydrolysates were prepared from C. reinhardtii. Among these, the alkaline protease hydrolysate (CRPA) demonstrated the most potent activity, exhibiting strong angiotensin-I converting enzyme (ACE) inhibitory activity in vitro and significant in vivo antihypertensive activity in spontaneously hypertensive rats (SHRs), with the effective dose corresponding to an estimated human-equivalent dose of 16 mg/kg/day. Using bioassay-guided isolation strategy, the first ACE-inhibitory peptide IDYRY (ID-5) was identified from C. reinhardtii, exhibiting an IC50 value of 18.54 +/- 5.57 mu M. ID-5 was characterized as a noncompetitive ACE inhibitor with confirmed antihypertensive activity both in vitro and in vivo. Molecular dynamics simulations revealed that ID-5 forms unique hydrogen bonds with Asp415 and Arg522, distinguishing its binding mechanism from that of captopril or lisinopril. Collectively, these findings highlight the enhanced bioactivity of CRPA and position C. reinhardtii as a sustainable microalgal source for developing functional foods and nutraceuticals aimed at blood pressure management.
WOS关键词ENZYME-INHIBITORY PEPTIDES ; BLOOD-PRESSURE ; ANGIOTENSIN ; IDENTIFICATION ; OPTIMIZATION ; PURIFICATION ; STRESS
资助项目Science and Technology Project of Fujian Province[2024 T3057] ; Self-Deployed Project of the Institute of Oceanology, Chinese Academy of Sciences[IOCASZZZX107] ; Oceanographic Data Center, Institute of Oceanology, Chinese Academy of Sciences ; Core Technology Facility of the Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences CAS
WOS研究方向Food Science & Technology
语种英语
WOS记录号WOS:001676302500001
出版者ELSEVIER
源URL[http://ir.qdio.ac.cn/handle/337002/204646]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Yue, Yang; Zhang, Quanbin
作者单位1.Chinese Acad Sci, Inst Oceanol, Lab Expt Marine Biol, Qingdao 266000, Peoples R China
2.Qingdao Marine Sci & Technol Ctr, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China
3.Univ Chinese Acad Sci, Beijing, Peoples R China
推荐引用方式
GB/T 7714		 Suo, Qishan,Yue, Yang,Wang, Jing,et al. Discovery and molecular mechanism of a novel antihypertensive peptide from Chlamydomonas reinhardtii based on molecular docking, molecular dynamics simulation, in vitro, and in vivo analysis[J]. FOOD RESEARCH INTERNATIONAL,2026,229:13.
APA Suo, Qishan,Yue, Yang,Wang, Jing,Wu, Ning,Geng, Lihua,&Zhang, Quanbin.(2026).Discovery and molecular mechanism of a novel antihypertensive peptide from Chlamydomonas reinhardtii based on molecular docking, molecular dynamics simulation, in vitro, and in vivo analysis.FOOD RESEARCH INTERNATIONAL,229,13.
MLA Suo, Qishan,et al."Discovery and molecular mechanism of a novel antihypertensive peptide from Chlamydomonas reinhardtii based on molecular docking, molecular dynamics simulation, in vitro, and in vivo analysis".FOOD RESEARCH INTERNATIONAL 229(2026):13.

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来源：海洋研究所

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