201. Study on the interaction between florasulam and bovine serum albumin
- Author
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Jinghe Yang, Xia Wu, Jinhua Zheng, Haiping Zhou, Yongjun Tang, Dehuan Ran, and Meifeng Zhang
- Subjects
Circular dichroism ,Sociology and Political Science ,Protein Conformation ,Clinical Biochemistry ,Serum albumin ,Analytical chemistry ,In Vitro Techniques ,Biochemistry ,medicine ,Animals ,Bovine serum albumin ,Spectroscopy ,Sulfonamides ,Quenching (fluorescence) ,Binding Sites ,biology ,Hydrogen bond ,Chemistry ,Circular Dichroism ,Tryptophan ,Serum Albumin, Bovine ,Human serum albumin ,Binding constant ,Fluorescence ,Clinical Psychology ,Crystallography ,Pyrimidines ,Spectrometry, Fluorescence ,Energy Transfer ,biology.protein ,Thermodynamics ,Cattle ,Spectrophotometry, Ultraviolet ,Law ,Social Sciences (miscellaneous) ,medicine.drug - Abstract
In this paper, the interaction between florasulam (FU, 2',6',8-trifluoro-5-methoxy [Kragh-Hansen U, Molecular aspects of ligand binding to serum albumin. Pharmacol Rev 33(1):17-53 1981; Carter DC and Ho JX, Structure of serum albumin. Adv Protein Chem 45:153-203 1994; He XM, and Carter DC, Atomic structure and chemistry of human serum albumin. Nature 358(6383):209-215 1992] triazolo [1,5-c]pyrimidine-2-sulfonanilide) and bovine serum albumin (BSA) was investigated by fluorescence, ultraviolet absorption (UV) and Far-UV circular dichroism (CD) spectrometries. A strong fluorescence quenching was observed and the quenching mechanism was considered as static quenching. The binding constant of FU with BSA at 299 and 309 K were obtained as 1.5 x 10(4) and 7.1 x 10(3) l mol(-1), respectively. There was one binding site between FU and BSA. The thermodynamic parameters enthalpy change (DeltaH) and entropy change (DeltaS) were calculated as -57.89 kJ mol(-1) and -113.6 J mol(-1) K(-1), respectively, which indicated that the acting force between FU and BSA was mainly hydrogen bond and Van der Waals force. According to the Förster non-radiation energy transfer theory, the average binding distance between donor (BSA) and acceptor (FU) was obtained (r = 1.59 nm). The investigations of the UV/Vis and CD spectra of the system showed that the conformation of BSA was changed in presence of FU.
- Published
- 2007