Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki-Reference-Cited by-同舟云学术

Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki

Published:2023-08-21 Issue:8 Volume:21 Page:458
ISSN:1660-3397
Container-title:Marine Drugs
language:en
Short-container-title:Marine Drugs

Author:

Heo Seong-Yeong¹²,Kang Nalae¹,Kim Eun-A¹,Kim Junseong¹,Lee Seung-Hong³,Ahn Ginnae⁴,Oh Je Hyeok⁵^ORCID,Shin A Young⁵,Kim Dongsung⁵,Heo Soo-Jin¹²

Affiliation:

1. Jeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju 63349, Republic of Korea

2. Department of Marine Biotechnology, University of Science and Technology (UST), Daejeon 34113, Republic of Korea

3. Department of Pharmaceutical Engineering, Soonchunhyang University, Asan 31538, Republic of Korea

4. Department of Food Technology and Nutrition, Chonnam National University, Yeosu 59626, Republic of Korea

5. Marine Ecosystem and Biological Research Center, Korea Institute of Ocean Science and Technology (KIOST), Busan 49111, Republic of Korea

Abstract

The objective of this study was to prepare an angiotensin I-converting enzyme (ACE)-inhibitory peptide from the hydrothermal vent mussel, Gigantidas vrijenhoeki. The G. vrijenhoeki protein was hydrolyzed by various hydrolytic enzymes. The peptic hydrolysate exhibited the highest ACE-inhibitory activity and was fractionated into four molecular weight ranges by ultrafiltration. The <1 kDa fraction exhibited the highest ACE inhibitory activity and was found to have 11 peptide sequences. Among the analyzed peptides, KLLWNGKM exhibited stronger ACE inhibitory activity and an IC50 value of 0.007 μM. To investigate the ACE-inhibitory activity of the analyzed peptides, a molecular docking study was performed. KLLWNGKM exhibited the highest binding energy (−1317.01 kcal/mol), which was mainly attributed to the formation of hydrogen bonds with the ACE active pockets, zinc-binding motif, and zinc ion. These results indicate that G. vrijenhoeki-derived peptides can serve as nutritional and pharmacological candidates for controlling blood pressure.

Funder

Korea Institute of Marine Science & Technology

Publisher

MDPI AG

Subject

Drug Discovery,Pharmacology, Toxicology and Pharmaceutics (miscellaneous),Pharmaceutical Science

Link

https://www.mdpi.com/1660-3397/21/8/458/pdf

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