Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki
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Title
- Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki
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Author(s)
- Heo, Seong Yeong; Kang, Na Lae; Kim, Eun A; Kim, Jun Seong; Lee, Seung-Hong; Ahn, Ginnae; Oh, Je Hyeok; Shin, A Young; Kim, Dong Sung; Heo, Soo Jin
- KIOST Author(s)
- Heo, Seong Yeong(허성영); Kang, Na Lae(강나래); Kim, Eun A(김은아); Kim, Jun Seong(김준성); Oh, Je Hyeok(오제혁); Shin, A Young(신아영); Kim, Dong Sung(김동성); Heo, Soo Jin(허수진)
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Alternative Author(s)
- 허성영; 강나래; 김은아; 김준성; 오제혁; 신아영; 김동성; 허수진
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Publication Year
- 2023-08
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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.
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ISSN
- 1660-3397
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/44506
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DOI
- 10.3390/md21080458
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Bibliographic Citation
- Marine Drugs, v.21, no.8, 2023
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Publisher
- Multidisciplinary Digital Publishing Institute (MDPI)
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Keywords
- hydrothermal vent mussel; Gigantidas vrijenhoeki; angiotensin I-converting enzyme; molecular docking; bioactive peptide
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Type
- Article
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Language
- English
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Document Type
- Article
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