alexa Study on the Interaction of Retinoic Acids to Human Serum Albumin by Fluorescence and Circular Dichroism Spectroscopy
ISSN: 2380-2391

Journal of Environmental Analytical Chemistry
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Research Article

Study on the Interaction of Retinoic Acids to Human Serum Albumin by Fluorescence and Circular Dichroism Spectroscopy

Heyong Huang1,2, Xiansheng Liu1, Ruiming Han1 and Guoxiang Wang1*

1Jiangsu Key Laboratory of Environment Change and Ecological Construction, Jiangsu Center for Collaborative Innovation in Geographical Information Resource Development and Application, College of Geographical Science, Nanjing Normal University, Nanjing 210023, China

2Analysis and Testing Center, Nanjing Normal University, Nanjing 210023, China

*Corresponding Author:
Guoxiang Wang
Jiangsu Key Laboratory of Environment
Change and Ecological Construction
Jiangsu Center for Collaborative Innovation
in Geographical Information Resource
Development and Application
College of Geographical Science
Nanjing Normal University
Nanjing 210023, China
Tel:+8602585898176
E-mail: [email protected]

Received date: March 29, 2017; Accepted date: April 04, 2017; Published date: April 07, 2017

Citation: Huang H, Liu X, Han R, Wang G (2017) Study on the Interaction of Retinoic Acids to Human Serum Albumin by Fluorescence and Circular Dichroism Spectroscopy. J Environ Anal Chem 4:192. doi:10.4172/2380-2391.1000192

Copyright: © 2017 Huang H, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Retinoic acids (RAs) are considered to be endocrine disruptor chemicals and toxic environmental priority pollutants. In this paper, the interactions between RAs and human serum albumin (HSA) were examined by steady state fluorescence, time-resolved fluorescence and circular dichroism spectroscopy (CD). The RAs quenched the fluorescence of the protein remarkably and the mechanism of quenching was found to be static in nature. Synchronous fluorescence studies suggested that the polarity around the tryptophan(Trp) residues and tyrosine(Tyr) residues was not altered in the presence of RAs. The thermodynamic parameters of the binding reactions (ΔGθ, ΔHθ, ΔSθ) were measured,and they indicated the presences of hydrophobic forces and hydrogen interactions in the RAs–HSA interactions. The alterations of HSA secondary structure in the presence of RAs were confirmed by CD and time resolved fluorescence spectroscopy.

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