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Xanthine oxidase inhibitory peptides derived from tuna protein: virtual screening, inhibitory activity, and molecular mechanisms
Author(s) -
Yu Zhipeng,
Kan Ruotong,
Wu Sijia,
Guo Hui,
Zhao Wenzhu,
Ding Long,
Zheng Fuping,
Liu Jingbo
Publication year - 2020
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.10745
Subject(s) - xanthine oxidase , chemistry , hyperuricemia , virtual screening , inhibitory postsynaptic potential , tetrapeptide , salt bridge , hydrogen bond , docking (animal) , peptide , biochemistry , uric acid , stereochemistry , enzyme , mutant , biology , molecule , drug discovery , organic chemistry , medicine , nursing , neuroscience , gene
BACKGROUND There has been growing interest in the use of xanthine oxidase (XO) as a therapeutic agent to prevent gout and hyperuricemia. In the present study, XO inhibitory peptides were identified from tuna protein by virtual screening, and molecular docking was used to elicit the interaction mechanism between XO and peptides. RESULTS A novel tetrapeptide, EEAK, exhibited high XO inhibitory activity with an IC 50 of 173.00 ± 0.06 μM. Molecular docking analysis revealed that EEAK bound with the pivotal residues of XO's active sites (i.e., Glu802, Arg880, Glu1261) through two conventional hydrogen bond interactions, two attractive charge interactions, and one salt bridge. EEAK could also bind with the residues Phe649, Leu648, Lys771, Ser876, Phe914, and Thr1010 of XO. CONCLUSION This study suggested that conventional hydrogen bond interactions and electrostatic interactions play an important role in XO inhibition. The novel XO inhibitory peptide EEAK from tuna protein could be used as potential candidate for controlling gout and hyperuricemia. © 2020 Society of Chemical Industry