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- W2356197214 abstract "The binding reaction of Sinomenine with bovine serum albumin was studied at 295K,303K,310K and 315K by fluorescence quenching spectra and synchronous fluorescence spectra.It was shown that Sinomenine has a strong ability of quenching the fluorescence of BSA.The Stern-Volmer curve of the fluorescence quenching of BSA by Sinomenine indicated that the quenching mechanism of Sinomenine to BSA was a static quenching process;According to the F?觟rster theory of non-radiation energy transfer,the binding distances(r) was 2.22 nm(310K).The thermodynamic parameters showed that the interaction of Sinomenine and BSA was mainly driven by hydrogen bonds and Vander Waals forces,and the synchronous spectrum was used to investigate the conformational changes of BSA." @default.
- W2356197214 created "2016-06-24" @default.
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- W2356197214 date "2010-01-01" @default.
- W2356197214 modified "2023-09-23" @default.
- W2356197214 title "Studies on the Interaction Between Sinomenine and Bovine Serum Albumin by Fluorescence Spectroscopy" @default.
- W2356197214 hasPublicationYear "2010" @default.
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