Study on the Interaction between Florasulam and Bovine Serum Albumin |
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Authors: | Dehuan Ran Xia Wu Jinhua Zheng Jinghe Yang Haiping Zhou Meifeng Zhang Yongjun Tang |
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Affiliation: | (1) Key Laboratory of Colloid and Interface Chemistry (Shandong University), Ministry of Education, School of Chemistry and Chemical Engineering, Shandong University, Jinan, 250100, Shandong, People’s Republic of China;(2) Shandong Pesticide Research Institute, Jinan, 250100, Shandong, People’s Republic of China |
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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?×?104 and 7.1?×?103 l mol?1, respectively. There was one binding site between FU and BSA. The thermodynamic parameters enthalpy change (ΔH) and entropy change (ΔS) 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. |
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Keywords: | Florasulam Bovine serum albumin Fluorescence quenching F?rster non-radiative energy transfer |
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