Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method.
The interaction between palmatine hydrochloride with human serum albumin (HSA) was investigated by fluorescence quenching technique and UV/vis absorption spectroscopy. The results of fluorescence titration revealed that palmatine hydrochloride could strongly quench the intrinsic fluorescence of HSA by static quenching and nonradiative energy transferring. The electrostatic interaction plays a major role in stabilizing the complex. The binding site number n and apparent binding constant KA, corresponding thermodynamic parameters DeltaG, DeltaH and DeltaS at different temperatures were calculated. The distance r between donor (HSA) and acceptor (palmatine hydrochloride) was obtained according to fluorescence resonance energy transfer. The effect of palmatine hydrochloride on the conformation of HSA was analyzed using synchronous fluorescence spectroscopy.
Wang
Yan-Qing
YQ
Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng Teachers College, Yancheng City, Jiangsu Province 224002, People's Republic of China. wyqing76@126.com
Zhang
Hong-Mei
HM
Zhang
Gen-Cheng
GC
D001600:Berberine Alkaloids / Q000378:metabolism*; D001665:Binding Sites; D005453:Fluorescence; D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D001600:Berberine Alkaloids; D012709:Serum Albumin; C005413:palmatine