Molecular simulation of the interaction between novel type rhodanine derivative probe and bovine serum albumin |
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Authors: | Jinghua Yu Bo Li Ping Dai Shenguang Ge |
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Institution: | aSchool of Chemistry and Chemical Engineering, University of Jinan, Jinan 250022, Shandong Province, People's Republic of China;bTianjin Cement Industry Design and Research Institute Co., Ltd, Tianjin 300400, People's Republic of China |
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Abstract: | The interaction between 3-(4′-methylphenyl)-5-(4′-methyl-2′-sulfophenylazo) rhodanine (M4MRASP) and bovine serum albumin (BSA) was studied by using spectrofluorimetry. It was shown in fluorescence spectrums that the quenching mechanism of BSA by M4MRASP was a static quenching. Meanwhile, the binding constant and binding site numbers were calculated. The action distance (r = 8.03 nm) and energy transfer efficiency (E = 0.12) between donor (BSA) and acceptor (M4MRASP) were obtained according to the theory of Förster non-radiation energy transfer. The effect of M4MRASP on the conformation of BSA was further analyzed by using synchronous fluorescence spectrometry. A new model of the interaction between small organic molecule and biomacromolecule was established. The results offered a reference for the studies on the biological effects and action mechanism of small molecule with protein. |
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Keywords: | Fluorescence spectrum Rhodanine derivative Bovine serum albumin Interaction |
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