[Studies on the interaction between alpinetin and human serum albumin by fluorescence spectroscopy].
The interaction between alpinetin and human serum albumin (HSA) was studied by fluorescence and UV/Vis absorption spectroscopy. The results revealed that alpinetin caused the fluorescence quenching of HSA through a dynamic quenching procedure. The quenching constant was obtained at various temperatures. The binding locality was found to be an area 4.05 nm away from tryptophan residue in HSA based on Forster's non-radiation energy transfer mechanism. The binding power between alpinetin and HSA is mainly the hydrophobic interaction according to the thermodynamic parameters. The effect of alpinetin on the conformation of HSA was analyzed by three-dimensional fluorescence spectra, contour spectra and synchronous spectra.
Zhang
Guo-Wen
GW
State Key Laboratory of Food Science and Technique, Nanchang University, Nanchang 330047, China. gwzhang@ncu.edu.cn
Wang
An-Ping
AP
Jiang
Ting
T
D044950:Flavanones / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D012709:Serum Albumin / Q000032:analysis* / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013053:Spectrophotometry; D013816:Thermodynamics
D044950:Flavanones; D012709:Serum Albumin; C436748:alpinetin