Chiral discrimination and interaction mechanism between enantiomers and serum albumins. Issue 4 (4th March 2013)

• Record Type: Journal Article
• Authors: Fang, ZhiLi; Su, WenCui; Zhang, WeiGuang; Xu, Yan; Xiong, YaJin; Luo, MiaoLi; Fan, Jun; Yin, Xia
• Is Part Of: Journal of molecular recognition. Volume 26:Issue 4(2013:Apr.)
• Page Start: 161
• Page End: 164
• Publication Date: 2013-03-04
• Subjects: chiral discrimination -- enantiomers -- interaction mechanism -- serum albumin; Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2247
• Languages: English
• ISSNs: 0952-3499

Abstract

Abstract : The chiral discrimination studies of biological system are theoretically and practically significant for the development of chiral drugs and life science. Our work has embarked upon the interaction between serum albumin (SA) (including human SA and bovine SA), R, S ‐1‐(4‐methoxyphenyl)ethylamine, and R, S ‐1‐(3‐methoxyphenyl)ethylamine. The formation of intermediate transition state, binding sites, and chiral discrimination ability can be investigated by ultraviolet‐visible spectra and fluorescence spectra. Moreover, both the changes of hydrophobic microenvironment and energy transfer can be detected by synchronous fluorescence spectra and fluorescence lifetime. Copyright © 2013 John Wiley & Sons, Ltd. Abstract : Our group has embarked upon the investigated the chiral discrimination and enantioselective interaction between SA and R, S‐4‐MPEA, R, S‐3‐MPEA by spectroscopic methods. UV‐vis and FL spectra can be used to investigate the formation of intermediate transition state, binding sites and chiral discrimination ability. Furthermore, synchronous fluorescence spectra and fluorescence lifetime could provide some information on both the changes of hydrophobic microenvironment and energy transfer.