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Spectrochim Acta A Mol Biomol Spectrosc. 2011 Jan;78(1):443-8. doi: 10.1016/j.saa.2010.11.007. Epub 2010 Nov 23.

Spectrophotometric study of the interaction between chlorotetracycline and bovine serum albumin using Eosin Y as site marker with the aid of chemometrics.

Author information

1
Stake Laboratory of Food Science and Technology, Department of Chemistry, Nanchang University, Nanchang, Jiangxi 330031, China. ynni@ncu.edu.cn

Abstract

Interaction of chlorotetracycline (CTC) with bovine serum albumin (BSA) was investigated under simulated physiological conditions by spectroscopy with the aid of multivariate curve resolution-alternating least squares (MCR-ALS). Eosin Y was selected as an alternative site I marker on the BSA to study the above molecular interaction. The binding of Eosin Y and CTC to BSA showed that CTC was displaced from CTC-BSA complex by Eosin Y, and Eosin Y-BSA complex was formed. However, the recorded fluorescence spectra of Eosin Y and Eosin Y-BSA overlapped and MCR-ALS was applied to resolve the two-way fluorescence spectra. From the resolved equilibrium concentration profiles, it was observed that Eosin Y competed with CTC in the binding process with BSA; it was also shown that the binding site of CTC on BSA was site I, and this was further confirmed by the fluorescence polarization method. Compared with some common site I markers for BSA, the fluorescence and UV-vis spectral shapes of the Eosin Y-BSA complex were quite different from that of Eosin Y, and this feature facilitated the investigation of the small molecule-BSA interaction.

PMID:
21163687
DOI:
10.1016/j.saa.2010.11.007
[Indexed for MEDLINE]
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