Interaction between isorhamnetin or taxifolin and human serum albumin
The interaction of two structurally similar flavonoids,isorhamnetin or taxifolin with human serum albumin(HSA)were investigated by fluorescence spectroscopy,CD spectroscopy and computer simulation techniques.Their binding properties,binding sites,binding modes and the effects on the conformation of HSA were determined.The fluorescence spectra showed that isorhamnetin or taxifolin formed a stable complex with HSA,and binding constants reached 105 L·mol-1,hydrogen bonds and hydrophobic force were the main binding forces.The sites competition experiments and molecular docking showed that the site Ⅰ of subdomain IIA in HSA was the main binding site of isorhamnetin or taxifolin.Synchronous fluorescence,CD spectra,surface hydrophobicity experiments and molecular dynamics simulations indicated that the binding of isorhamnetin or taxifolin induced the conformational changes of HSA,and the polypeptide skeleton was partially extended.
human serum albuminisorhamnetintaxifolininteraction
NETL
NSTL
万方数据
