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Purification,characterization and anti-hyperuricemic mechanism of novel xanthine oxidase inhibitory peptides from tea(Camellia sinensis L.)protein
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作者 Feng Ma Shili Sun +5 位作者 haoduo ye Zhenyu Zhang Qimiao Chen Shouwei Yin Yong Cao Jianyin Miao 《Food Bioscience》 2024年第5期719-734,共16页
In this study,two novel xanthine oxidase inhibitory peptides,PDEAVAYG(820.3602 Da)and IAAGLQNTG(843.4450 Da),were purified and identified from tea protein hydrolysate,and their IC_(50) values were 0.09 mg/mL(109.71μM... In this study,two novel xanthine oxidase inhibitory peptides,PDEAVAYG(820.3602 Da)and IAAGLQNTG(843.4450 Da),were purified and identified from tea protein hydrolysate,and their IC_(50) values were 0.09 mg/mL(109.71μM)and 0.24 mg/mL(284.55μM),respectively.During the gastrointestinal simulation digestion,PDEAVAYG was broken down into new peptides,while IAAGLQNTG exhibited some stability.Molecular docking results showed that hydrogen bonding,π-πstacking,and hydrophobic interactions exerted crucial effects on the interaction between peptides and xanthine oxidase.In the hyperuricemia cell model,compared to the model group,1.0 mg/mL of PDEAVAYG and IAAGLQNTG decreased cellular uric acid levels by 40.80%and 33.33%,respectively.The RNA-seq experiments revealed that PDEAVAYG could alleviate hyperuricemia by regulating mRNA expression for pro-inflammatory factors,growth factors associated with cardiovascular disease,and uric acid efflux transporter proteins in cells.This study provides a new theoretical reference for the development of functional foods or nutritional supplements using peptides with anti-hyperuricemic activity. 展开更多
关键词 Tea(Camellia sinensis L.)protein Xanthine oxidase inhibitory peptides Anti-hyperuricemic activity Molecular docking Hyperuricemia cell model Activity mechanism
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