Discovery of a novel nanomolar angiotensin-I converting enzyme inhibitory peptide with unusual binding mechanisms derived from Chlorella pyrenoidosa
文献类型：期刊论文
| 作者 | Suo, Qishan1,2,3 ; Wang, Jing1,2; Wu, Ning1,2; Geng, Lihua1,2; Zhang, Quanbin1,2,3; Yue, Yang1,2
|
| 刊名 | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
 |
| 出版日期 | 2024-11-01 |
| 卷号 | 280页码:13 |
| 关键词 | Angiotensin converting enzyme Chlorella peptide Molecular dynamic simulation |
| ISSN号 | 0141-8130 |
| DOI | 10.1016/j.ijbiomac.2024.135873 |
| 通讯作者 | Yue, Yang(yueyang@qdio.ac.cn) |
| 英文摘要 | Chlorella pyrenoidosa (C. pyrenoidosa) has been cultivated in large quantities and proven to be antihypertensive when consumed orally. However, the antihypertensive peptides derived from C. pyrenoidosa remains scarce. In this study, trypsin was chosen to prepare the hydrolysate of C. pyrenoidosa, which was then fractionated by column chromatography. And ninety-nine peptides were identified by LC-MS/MS, after which 10 peptides were chosen by docking-based virtual screening and demonstrated their ability to inhibit ACE. Among them, LVAKA (LV-5) had the lowest IC50 (26.66 mu M). LV-5, LKKAP, and PGLRP were identified as non-competitive ACE inhibitory peptides with significant stability under extreme pH and high temperatures conditions. Both in silico and in-vitro simulated gastrointestinal digestion revealed that these three peptides could release ACE inhibitory peptide fragments upon digestion. Sequence optimization of LV-5 led to the discovery of LRAKA (LR-5), which was identified as a novel nanomolar ACE peptide with an IC50 of 350 nM in-vitro and a potent antihypertensive peptide in-vivo. Moreover, molecular dynamic simulation indicated that LR-5 interacted with an unconventional binding site on ACE. These findings underscore the potential of Chlorella as a source of antihypertensive peptides and suggest a promising future for the use of Chlorella-derived peptides in hypertension management. |
| WOS关键词 | MOLECULAR DOCKING ; ACE ; PURIFICATION ; METAANALYSIS ; MICROALGAE ; COMPLEX |
| 资助项目 | Science and Technology Project of Fujian Province[2023T3034] ; Oceanographic Data Center, Institute of Oceanology, Chinese Academy of Sciences ; Core Technology Facility of Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences CAS |
| WOS研究方向 | Biochemistry & Molecular Biology ; Chemistry ; Polymer Science |
| 语种 | 英语 |
| WOS记录号 | WOS:001322231500001 |
| 出版者 | ELSEVIER |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/199210]  |
| 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 |
| 作者单位 | 1.Qingdao Marine Sci & Technol Ctr, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China 2.Chinese Acad Sci, Inst Oceanol, Ctr Ocean Megasci, CAS & Shandong Prov Key Lab Expt Marine Biol, Qingdao, Peoples R China 3.Univ Chinese Acad Sci, Beijing, Peoples R China |
| 推荐引用方式 GB/T 7714 | Suo, Qishan,Wang, Jing,Wu, Ning,et al. Discovery of a novel nanomolar angiotensin-I converting enzyme inhibitory peptide with unusual binding mechanisms derived from Chlorella pyrenoidosa[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2024,280:13. |
| APA | Suo, Qishan,Wang, Jing,Wu, Ning,Geng, Lihua,Zhang, Quanbin,&Yue, Yang.(2024).Discovery of a novel nanomolar angiotensin-I converting enzyme inhibitory peptide with unusual binding mechanisms derived from Chlorella pyrenoidosa.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,280,13. |
| MLA | Suo, Qishan,et al."Discovery of a novel nanomolar angiotensin-I converting enzyme inhibitory peptide with unusual binding mechanisms derived from Chlorella pyrenoidosa".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 280(2024):13. |
入库方式： OAI收割
来源：海洋研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。