期刊
FOOD CHEMISTRY
卷 272, 期 -, 页码 453-461出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2018.08.057
关键词
Hyperuricemic mice; Xanthine oxidase inhibition; Structure-activity relationship; Di-/tri-peptide; Molecular docking
This study follows recent attempts to discover natural xanthine oxidase (XO) inhibitors from foods, focusing herein on under-researched fish proteins. The anti-hyperuricemic function of tuna flesh hydrolysate (TPH) produced using Alcalase 2.4L was confirmed in potassium oxonate-induced hyperuricemic rats. TPH was separated using 80 wt% aqueous ethanol. The ethanol-soluble fraction (ESF) abundant in small peptides (< 1000 Da) afforded the highest XO inhibition. Separation of ESF by Sephadex G-15 and UPLC/MS/MS revealed 13 di-/tri-peptides (12 are newly identified XO inhibitors). Their XO inhibitory activities were assessed using corresponding synthetic peptides via an improved HPLC method. Results indicate that Phe-containing peptides were more potent XO inhibitors than Trp-containing peptides, with Phe-His having the highest XO inhibitory activity (IC50 = 25.7 mM). Molecular docking studies revealed the importance of two hydrogen bonds and one pi-pi stacking interaction with Phe-914 in XO for XO-peptide inhibitor binding. Phe-containing di-/tripeptides could be potent XO inhibitors against hyperuricemia.
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