Regulating inhibitory activity of potato I-type proteinase inhibitor from buckwheat by rutin and quercetin.
This study aims to investigate the effects of two flavonoids, rutin and quercetin, on inhibitory activity of recombinant buckwheat trypsin inhibitor (rBTI). We found that rutin and quercetin could quench the florescence of rBTI through the static quenching process. We also observed that upon binding to rutin or quercetin, rBTI underwent conformational changes. The results also suggested that rutin and quercetin bind to two different sites on rBTI through different interactions: rutin binds to rBTI through van der Waals forces and hydrogen bonds, whereas quercetin binds through hydrophobic interactions. Rutin and quercetin also markedly deactivated the trypsin inhibitory activity (TIA) of rBTI, while quercetin exhibited higher inactivation effect on rBTI than rutin due to its structure. Finally, the molecular docking revealed the molecular binding between the flavonoids and rBTI. These findings can be useful for the understanding of how flavonoid affects the inhibitory of rBTI.
['Cui|Xiaodong|X|0000-0002-2280-4160', 'Lv|Yifan|Y|', 'Wang|Zhuanhua|Z|', 'Li|Jiao|J|', 'Li|Chen|C|0000-0002-0863-9605']
D019612:Fagopyrum D062105:Molecular Docking Simulation D010447:Peptide Hydrolases D011794:Quercetin D012431:Rutin D011198:Solanum tuberosum
potato I-type proteinase inhibitor rutin quercetin binding interaction fluorescence quenching