Interaction of cromolyn sodium with human serum albumin: a fluorescence quenching study.
The interaction between cromolyn sodium (CS) and human serum albumin (HSA) was investigated using tryptophan fluorescence quenching. In the discussion of the mechanism, it was proved that the fluorescence quenching of HSA by CS is a result of the formation of a CS-HSA complex. Quenching constants were determined using the Sterns-Volmer equation to provide a measure of the binding affinity between CS and HSA. The thermodynamic parameters DeltaG, DeltaH, and DeltaS at different temperatures were calculated. The distance r between donor (Trp214) and acceptor (CS) was obtained according to fluorescence resonance energy transfer (FRET). Furthermore, synchronous fluorescence spectroscopy data and UV-vis absorbance spectra have suggested that the association between CS and HSA changed the molecular conformation of HSA and the electrostatic interactions play a major role in CS-HSA association.
Hu
Yan-Jun
YJ
Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Liu
Yi
Y
Pi
Zhen-Bang
ZB
Qu
Song-Sheng
SS
D004205:Cromolyn Sodium / Q000737:chemistry*; D004735:Energy Transfer; D006801:Humans; D015394:Molecular Structure; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D055672:Static Electricity
D012709:Serum Albumin; D004205:Cromolyn Sodium