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Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo

Neptunea arthritica cumingii (Nac) is a marine snail with high nutritional and commercial value; however, little is known about its active peptides. In this study, two multi-functional peptides, YSQLENEFDR (Tyr-Ser-Gln-Leu-Glu-Asn-Glu-Phe-Asp-Arg) and YIAEDAER (Tyr-Ile-Ala-Glu-Asp-Ala-Glu-Arg), were...

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Autores principales: Zhang, Shan-Shan, Han, Li-Wen, Shi, Yong-Ping, Li, Xiao-Bin, Zhang, Xuan-Ming, Hou, Hai-Rong, Lin, Hou-Wen, Liu, Ke-Chun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315844/
https://www.ncbi.nlm.nih.gov/pubmed/30486436
http://dx.doi.org/10.3390/md16120473
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author Zhang, Shan-Shan
Han, Li-Wen
Shi, Yong-Ping
Li, Xiao-Bin
Zhang, Xuan-Ming
Hou, Hai-Rong
Lin, Hou-Wen
Liu, Ke-Chun
author_facet Zhang, Shan-Shan
Han, Li-Wen
Shi, Yong-Ping
Li, Xiao-Bin
Zhang, Xuan-Ming
Hou, Hai-Rong
Lin, Hou-Wen
Liu, Ke-Chun
author_sort Zhang, Shan-Shan
collection PubMed
description Neptunea arthritica cumingii (Nac) is a marine snail with high nutritional and commercial value; however, little is known about its active peptides. In this study, two multi-functional peptides, YSQLENEFDR (Tyr-Ser-Gln-Leu-Glu-Asn-Glu-Phe-Asp-Arg) and YIAEDAER (Tyr-Ile-Ala-Glu-Asp-Ala-Glu-Arg), were isolated and purified from meat and visceral mass extracts of Nac using a multi-bioassay-guided method and were characterized by using liquid chromatography-tandem mass spectrometry. Both peptides showed high antioxidant, angiotensin-converting enzyme (ACE)-inhibitory, and anti-diabetic activities, with half-maximal effective concentrations values less than 1 mM. Antioxidant and ACE-inhibitory activities were significantly higher for YSQLENEFDR than for YIAEDAER. In a zebrafish model, the two peptides exhibited strong scavenging ability for reactive oxygen species and effectively protected skin cells against oxidative damage without toxicity. Molecular docking simulation further predicted the interactions of the two peptides and ACE. Stability analysis study indicated that the two synthetic peptides maintained their activities under thermal stress and simulated gastrointestinal digestion conditions. The low molecular weight, high proportion of hydrophobic and negatively-charged amino acids, and specific C-terminal and N-terminal amino acids may contribute to the observed bio-activities of these two peptides with potential application for the prevention of chronic noncommunicable diseases.
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spelling pubmed-63158442019-01-10 Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo Zhang, Shan-Shan Han, Li-Wen Shi, Yong-Ping Li, Xiao-Bin Zhang, Xuan-Ming Hou, Hai-Rong Lin, Hou-Wen Liu, Ke-Chun Mar Drugs Article Neptunea arthritica cumingii (Nac) is a marine snail with high nutritional and commercial value; however, little is known about its active peptides. In this study, two multi-functional peptides, YSQLENEFDR (Tyr-Ser-Gln-Leu-Glu-Asn-Glu-Phe-Asp-Arg) and YIAEDAER (Tyr-Ile-Ala-Glu-Asp-Ala-Glu-Arg), were isolated and purified from meat and visceral mass extracts of Nac using a multi-bioassay-guided method and were characterized by using liquid chromatography-tandem mass spectrometry. Both peptides showed high antioxidant, angiotensin-converting enzyme (ACE)-inhibitory, and anti-diabetic activities, with half-maximal effective concentrations values less than 1 mM. Antioxidant and ACE-inhibitory activities were significantly higher for YSQLENEFDR than for YIAEDAER. In a zebrafish model, the two peptides exhibited strong scavenging ability for reactive oxygen species and effectively protected skin cells against oxidative damage without toxicity. Molecular docking simulation further predicted the interactions of the two peptides and ACE. Stability analysis study indicated that the two synthetic peptides maintained their activities under thermal stress and simulated gastrointestinal digestion conditions. The low molecular weight, high proportion of hydrophobic and negatively-charged amino acids, and specific C-terminal and N-terminal amino acids may contribute to the observed bio-activities of these two peptides with potential application for the prevention of chronic noncommunicable diseases. MDPI 2018-11-27 /pmc/articles/PMC6315844/ /pubmed/30486436 http://dx.doi.org/10.3390/md16120473 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Shan-Shan
Han, Li-Wen
Shi, Yong-Ping
Li, Xiao-Bin
Zhang, Xuan-Ming
Hou, Hai-Rong
Lin, Hou-Wen
Liu, Ke-Chun
Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo
title Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo
title_full Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo
title_fullStr Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo
title_full_unstemmed Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo
title_short Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo
title_sort two novel multi-functional peptides from meat and visceral mass of marine snail neptunea arthritica cumingii and their activities in vitro and in vivo
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315844/
https://www.ncbi.nlm.nih.gov/pubmed/30486436
http://dx.doi.org/10.3390/md16120473
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