Journal
MARINE DRUGS
Volume 19, Issue 10, Pages -Publisher
MDPI
DOI: 10.3390/md19100538
Keywords
round scad (Decapterus maruadsi); hydrolysis; peptides; xanthine oxidase inhibitory; purification; identification
Categories
Funding
- Key-Area Research and Development Program of Guangdong Province [2020B1111030004]
- Guangdong Basic and Applied Basic Research Foundation [2019A1515011588]
- China Agriculture Research System of MOF and MARA [CARS-47]
- Pearl River S&T Nova Program of Guangzhou [201906010081]
- Special Scientific Research Funds for Central Non-profit Institutes, Chinese Academy of Fishery Sciences [2020TD69]
- Central Public-interest Scientific Institution Basal Research Funds, South China Sea Fisheries Research Institute, CAFS [2021SD06]
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The study investigated the XO inhibitory effects of peptides purified from round scad hydrolysates, revealing FPSV and FPFP peptides to exhibit strong inhibitory activity. Fluorescence quenching mechanism and inhibition kinetics indicated their reversible and mixed-type inhibition. Molecular docking highlighted the importance of π-π stacking in the XO inhibitory activity of the peptides.
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 & PLUSMN; 1.81% and 20.09 & PLUSMN; 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 pi-pi stacking between Phe residue (contained in peptides) and Phe(914) (contained in the XO) in the XO inhibitory activity of the peptides.
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