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Study on the Interaction Between Nimesulide andBovine Serum Albumin by Spectrometry(PDF)

《南京师大学报（自然科学版）》[ISSN:1001-4616/CN:32-1239/N]

Issue:
2016年02期
Page:
50-
Research Field:
化学
Publishing date:

Info

Title:
Study on the Interaction Between Nimesulide andBovine Serum Albumin by Spectrometry
Author(s):
Liu Li; Cheng Feixiang
College of Chemistry and Chemical Engineering，Qujing Normal University，Qujing 655011，China
Keywords:
Nimesulide; fluorescence quenching; interaction
PACS:
O657.3
DOI:
10.3969/j.issn.1001-4616.2016.02.010
Abstract:
The interaction of Nimesulide（Nime）with bovine serum albumin（BSA）has been investigated by fluorescence，synchronous fluorescence，and ultraviolet-visible（UV-vis）spectrometry. The results indicated that（Nime）had a strong ability to quench the intrinsic fluorescence of BSA，while the fluorescence quenching was initiated by static quenching procedure. The analysis of synchronous fluorescence spectra showed the change in secondary structure of BSA upon interaction with Nime，leading to the polarity around BSA weakened. Site competitive experiments indicated that their binding to BSA primarily took place in subdomain IIA. There was some negative cooperative effect. For Nime，there was only one binding site on BSA. The values of negative enthalpy change and positive entropy change indicated that electrostatic interactions play an important role in the binding processes. In addition，the binding processes were spontaneous and carried out by exothermic reactions. Our results may have relevant insight into Nime’s clinical?application and efficacy.

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Last Update: 2016-06-30