Zexuan Xu,Miaoyu Gan,Weiliang Guan,Fang Tian,Yuxi Wang,Jinjie Zhang,Luyun Cai
Hyperuricemia arises from imbalanced uric acid metabolism, contributing to gout and related chronic diseases. When traditional drugs are used to treat hyperuricemia, side effects are inevitable, which promotes the exploration of new bioactive compounds. Protein hydrolysates and peptides are gradually showing potential in the treatment of hyperuricemia. This study investigated the uric acid inhibitory activity of peptides extracted fromTrachurus japonicususing in silico and in vitro methods. We employed in silico virtual enzymolysis and experimental validation to identify bioactive peptides fromTrachurus japonicusproteins. Four peptides (DF, AGF, QPSF, and AGDDAPR) were comprehensively screened by molecular docking and database analysis. After solid-phase synthesis, the inhibitory effects of these peptides on hyperuricemia were further verified in vitro and at the cellular level. The results showed that all four peptides have good hyperuricemia-inhibiting activities. Molecular docking and molecular dynamics revealed that peptides DF and AGDDAPR affect the production of uric acid by binding to the active sites of urate transporter 1 (URAT1), glucose transporter 9 (GLUT9), and xanthine oxidase (XOD), while peptides QPSF and AGF mainly influence the XOD active site, confirming that it is feasible to rapidly screen hyperuricemia-inhibiting peptides by molecular docking.
Resveratrol has a variety of physiological activities, but its bioavailability in the body is low. In this study, the interaction between the peptide SH, prepared from Scomberomorus niphonius, and resveratrol was judged by fluorescence spectroscopy. Then, SHa1 was obtained by the purification of SH, and its effect on the characteristics of resveratrol was studied. SHa1 interacted with resveratrol at 37 °C for 30 min to obtain the complex SHa1-R, which then showed an obviously stronger inhibition on B16 cells than resveratrol using the MTT assay after in vitro gastrointestinal digestion. The solubility and digestive stability of SHa1-R were higher than that of free resveratrol. The intestinal absorption rate of SHa1-R was also increased compared with resveratrol according to the non-inverted rat intestinal sac model. The structure of SHa1 was analyzed by UPLC, auto amino acid analysis, and UPLC-MS/MS. The molecular weight of SHa1 was mainly concentrated under 1000 Da, and it was rich in glutamic acid, aspartic acid, lysine, and leucine. Eighteen possible peptides were identified from SHa1. The results suggested that the peptide SHa-1 may help to increase the bioavailability of resveratrol by increasing the solubility, digestive stability and intestinal absorption of resveratrol, thereby promoting its inhibitory effect on B16 cells.
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