期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 13, 期 24, 页码 6609-6614出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2005.07.039
关键词
cromolyn sodium; human serum albumin; fluorescence quenching; thermodynamic parameters; fluorescence resonance energy transfer
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 Delta G, Delta H, and Delta S at different temperatures were calculated. The distance r between donor (Trp(214)) 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. (c) 2005 Elsevier Ltd. All rights reserved.
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