| Literature DB >> 20655275 |
Shuang Li1, Kelong Huang, Ming Zhong, Jun Guo, Wei-zheng Wang, Ronghua Zhu.
Abstract
The substitution of the hydrogen on aromatic and esterification of carboxyl group of the phenol compounds plays an important role in their bio-activities. In this paper, caffeic acid (CaA), chlorogenic acid (ChA) and ferulic acid (FA) were selected to investigate the binding to bovine serum albumin (BSA) using UV absorption spectroscopy, fluorescence spectroscopy and synchronous fluorescence spectroscopy. It was found that the methoxyl group substituting for the 3-hydroxyl group of CaA decreased the affinity for BSA and the esterification of carboxyl group of CaA with quinic acid increased the affinities. The affinities of ChA and FA with BSA were more sensitive to the temperature than that of CaA with BSA. Synchronous fluorescence spectroscopy and time-resolved fluorescence indicated that the Stern-Volmer plots largely deviated from linearity at high concentrations and were caused by complete quenching of the tyrosine fluorescence of BSA.Entities:
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Year: 2010 PMID： 20655275 DOI： 10.1016/j.saa.2010.04.026
Source DB: PubMed Journal: Spectrochim Acta A Mol Biomol Spectrosc ISSN： 1386-1425 Impact factor: 4.098