Screening and Molecular Mechanisms of Novel ACE-Inhibitory Peptides from <i>Gracilariopsis lemaneiformis</i>

Yongchang Su; Shicheng Chen; Jiashen Shen; Zhiwei Yi; Shuji Liu; Shuilin Cai; Nan Pan; Kun Qiao; Xiaoting Chen; Bei Chen; Min Xu; Suping Yang; Zhiyu Liu

doi:10.3390/ijms232314850

International Journal of Molecular Sciences (Nov 2022)

Screening and Molecular Mechanisms of Novel ACE-Inhibitory Peptides from <i>Gracilariopsis lemaneiformis</i>

Yongchang Su,
Shicheng Chen,
Jiashen Shen,
Zhiwei Yi,
Shuji Liu,
Shuilin Cai,
Nan Pan,
Kun Qiao,
Xiaoting Chen,
Bei Chen,
Min Xu,
Suping Yang,
Zhiyu Liu

Affiliations

Yongchang Su: College of Chemical Engineering, Huaqiao University, Xiamen 361021, China
Shicheng Chen: Department of Clinical and Diagnostic Sciences, School of Health Sciences, Oakland University, Rochester, MI 48309, USA
Jiashen Shen: College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China
Zhiwei Yi: Technology Innovation Center for Exploitation of Marine Biological Resources, Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China
Shuji Liu: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China
Shuilin Cai: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China
Nan Pan: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China
Kun Qiao: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China
Xiaoting Chen: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China
Bei Chen: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China
Min Xu: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China
Suping Yang: College of Chemical Engineering, Huaqiao University, Xiamen 361021, China
Zhiyu Liu: Key Laboratory of Cultivation and High-Value Utilization of Marine Organisms in Fujian Province, National Research and Development Center for Marine Fish Processing (Xiamen), Fisheries Research Institute of Fujian, Xiamen 361013, China

DOI: https://doi.org/10.3390/ijms232314850
Journal volume & issue: Vol. 23, no. 23
p. 14850

Abstract

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Candidate peptides with novel angiotensin-I-converting enzyme (ACE) inhibitor activity were obtained from hydrolysates of Gracilariopsis lemaneiformis by virtual screening method. Our results showed that G. lemaneiformis peptides (GLP) could significantly lower blood pressure in spontaneously hypertensive rats (SHR). At least 101 peptide sequences of GLP were identified by LC-MS/MS analysis and subjected to virtual screening. A total of 20 peptides with the highest docking score were selected and chemically synthesized in order to verify their ACE-inhibitory activities. Among them, SFYYGK, RLVPVPY, and YIGNNPAKG showed good effects with IC50 values of 6.45 ± 0.22, 9.18 ± 0.42, and 11.23 ± 0.23 µmoL/L, respectively. Molecular docking studies revealed that three peptides interacted with the active center of ACE by hydrogen bonding, hydrophobic interactions, and electrostatic forces. These peptides could form stable complexes with ACE. Furthermore, SFYYGK, RLVPVPY, and YIGNNPAKG significantly reduced systolic blood pressure (SBP) in SHR. YIGNNPAKG exhibited the highest antihypertensive effect, with the largest decrease in SBP (approximately 23 mmHg). In conclusion, SFYYGK, RLVPVPY, and YIGNNPAKG can function as potent therapeutic candidates for hypertension treatment.

Published in International Journal of Molecular Sciences

ISSN: 1661-6596 (Print); 1422-0067 (Online)
Publisher: MDPI AG
Country of publisher: Switzerland
LCC subjects: Science: Biology (General); Science: Chemistry
Website: http://www.mdpi.com/journal/ijms

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