Interaction mechanism of icariin and whey protein based on spectrofluorimetry and molecular docking

Abstract Icariin has low bioavailability and poor stability, which limits its wide application. The complexation of icariin and whey protein is expected to solve this problem, but there is no research on their interaction mechanism. In view of this, the related mechanism was studied systematically by spectrofluorimetry and molecular docking method in this study. The fluorescence analysis showed that icariin and whey protein could form a non-covalent complex driven by hydrophobic force, which led to the fluorescence quenching of whey protein. In this process, the microenvironment around the tyrosine residue and tryptophan residue of whey protein changed. The molecular docking analysis confirmed the existence of hydrophobic interaction and hydrogen bonding in the complex, which well confirmed fluorescence results. The obtained results can promote the application of icariin in food.

Bibliographic Details

Main Authors:	LI,Gang, GE,Xiaohong
Format:	Digital revista
Language:	English
Published:	Sociedade Brasileira de Ciência e Tecnologia de Alimentos 2023
Online Access:	http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612023000100438
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