Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard

Abstract

Auxis thazard meat was hydrolyzed by alkaline protease. Auxis thazard hydrolysate (ATH) obtained was isolated by ultrafiltration, size exclusion chromatography and reversed-phase high-performance liquid chromatography. Two peptides with high XOD inhibitory activity purified from ATH were identified as Pro-Asp-Leu (PDL, 344.87 Da) and Ser-Val-Gly-Gly-Ala-Leu (SVGGAL, 504.26 Da) by UPLC-MS/MS, which possessed high in vitro XOD inhibitory activity with the IC 50 values of 4.37 ± 0.11 mg mL -1 and 5.59 ± 0.09 mg mL -1 , respectively. Molecular simulation indicated that PDL and SVGGAL binded to XOD mainly through hydrogen bond and hydrophobic interaction, thereby inhibiting XOD activity. The research results suggested that the two peptides had potential application prospects as a safe XOD inhibitor substance for hyperuricemia treatment.

CRISPR/Cas9 System-Mediated Multi-copy Expression of an Alkaline Serine Protease in Aspergillus niger for the Production of XOD-Inhibitory Peptides

“…It has proved to be an efficient protease for the preparation of protein hydrolysates with XOD-inhibitory activity from different protein sources in the food industry . The Auxis thazard meat was hydrolyzed by alcalase to produce the XOD-inhibitory activity with IC 50 values ranging from 11.23 to 20.50 mg/mL . The tuna protein hydrolysates prepared by alcalase showed high XOD-inhibitory activity, and the IC 50 value of dipeptide FH was 25.7 mM .…”

“…7 The Auxis thazard meat was hydrolyzed by alcalase to produce the XODinhibitory activity with IC 50 values ranging from 11.23 to 20.50 mg/mL. 37 The tuna protein hydrolysates prepared by alcalase showed high XOD-inhibitory activity, and the IC 50 value of dipeptide FH was 25.7 mM. 38 Walnut meals and degreased walnut meals were hydrolyzed by alcalase.…”