2012
DOI: 10.1016/j.cclet.2012.02.003
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Studies on the binding of vinpocetine to human serum albumin by molecular spectroscopy and modeling

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Cited by 11 publications
(2 citation statements)
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“…The peak of BSA was slightly red shifted and decreased, which showed that the microenvironment around BSA was changed due to the V 18 . There are two kinds of fluorescence quenching, including dynamic and static quenching [ 20 , 21 ]. Due to the results, the absorbance peak of BSA was reduced by V 18 , and the fluorescence quenching of V 18 to BSA was likely to be static quenching.…”
Section: Resultsmentioning
confidence: 99%
“…The peak of BSA was slightly red shifted and decreased, which showed that the microenvironment around BSA was changed due to the V 18 . There are two kinds of fluorescence quenching, including dynamic and static quenching [ 20 , 21 ]. Due to the results, the absorbance peak of BSA was reduced by V 18 , and the fluorescence quenching of V 18 to BSA was likely to be static quenching.…”
Section: Resultsmentioning
confidence: 99%
“…However, the mechanism of interaction between VCM and protein is poorly understood. In a previous paper, we reported optical spectroscopic studies designed to characterize the interaction of vinpocetine (VPC) with HSA . VPC, a semi‐synthetic alkaloid derivative of VCM, is a cerebrovascular drug with a structure similar to that of VCM.…”
Section: Introductionmentioning
confidence: 99%