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Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates
The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad (Decapterus maruadsi) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them,...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8538066/ https://www.ncbi.nlm.nih.gov/pubmed/34677437 http://dx.doi.org/10.3390/md19100538 |
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author | Hu, Xiao Zhou, Ya Zhou, Shaobo Chen, Shengjun Wu, Yanyan Li, Laihao Yang, Xianqing |
author_facet | Hu, Xiao Zhou, Ya Zhou, Shaobo Chen, Shengjun Wu, Yanyan Li, Laihao Yang, Xianqing |
author_sort | Hu, Xiao |
collection | PubMed |
description | The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad (Decapterus maruadsi) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them, the RSHs of 6-h hydrolysis by neutrase displayed the strongest XO inhibitory activity and had an abundance of small peptides (<500 Da). Four novel peptides were purified by immobilized metal affinity chromatography and identified by nano-high-performance liquid chromatography mass/mass spectrometry. Their amino acid sequences were KGFP (447.53 Da), FPSV (448.51 Da), FPFP (506.59 Da) and WPDGR (629.66 Da), respectively. Then the peptides were synthesized to evaluate their XO inhibitory activity. The results indicated that the peptides of both FPSV (5 mM) and FPFP (5 mM) exhibited higher XO inhibitory activity (22.61 ± 1.81% and 20.09 ± 2.41% respectively). Fluorescence spectra assay demonstrated that the fluorescence quenching mechanism of XO by these inhibitors (FPSV and FPFP) was a static quenching procedure. The study of inhibition kinetics suggested that the inhibition of both FPSV and FPFP was reversible, and the type of their inhibition was a mixed one. Molecular docking revealed the importance of π-π stacking between Phe residue (contained in peptides) and Phe(914) (contained in the XO) in the XO inhibitory activity of the peptides. |
format | Online Article Text |
id | pubmed-8538066 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-85380662021-10-24 Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates Hu, Xiao Zhou, Ya Zhou, Shaobo Chen, Shengjun Wu, Yanyan Li, Laihao Yang, Xianqing Mar Drugs Article The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad (Decapterus maruadsi) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them, the RSHs of 6-h hydrolysis by neutrase displayed the strongest XO inhibitory activity and had an abundance of small peptides (<500 Da). Four novel peptides were purified by immobilized metal affinity chromatography and identified by nano-high-performance liquid chromatography mass/mass spectrometry. Their amino acid sequences were KGFP (447.53 Da), FPSV (448.51 Da), FPFP (506.59 Da) and WPDGR (629.66 Da), respectively. Then the peptides were synthesized to evaluate their XO inhibitory activity. The results indicated that the peptides of both FPSV (5 mM) and FPFP (5 mM) exhibited higher XO inhibitory activity (22.61 ± 1.81% and 20.09 ± 2.41% respectively). Fluorescence spectra assay demonstrated that the fluorescence quenching mechanism of XO by these inhibitors (FPSV and FPFP) was a static quenching procedure. The study of inhibition kinetics suggested that the inhibition of both FPSV and FPFP was reversible, and the type of their inhibition was a mixed one. Molecular docking revealed the importance of π-π stacking between Phe residue (contained in peptides) and Phe(914) (contained in the XO) in the XO inhibitory activity of the peptides. MDPI 2021-09-24 /pmc/articles/PMC8538066/ /pubmed/34677437 http://dx.doi.org/10.3390/md19100538 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Hu, Xiao Zhou, Ya Zhou, Shaobo Chen, Shengjun Wu, Yanyan Li, Laihao Yang, Xianqing Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates |
title | Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates |
title_full | Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates |
title_fullStr | Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates |
title_full_unstemmed | Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates |
title_short | Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates |
title_sort | purification and identification of novel xanthine oxidase inhibitory peptides derived from round scad (decapterus maruadsi) protein hydrolysates |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8538066/ https://www.ncbi.nlm.nih.gov/pubmed/34677437 http://dx.doi.org/10.3390/md19100538 |
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