期刊名称：Journal of Environmental Analytical Chemistry
电子版ISSN：2380-2391
出版年度：2017
卷号：4
期号：2
页码：1-7
DOI：10.4172/2380-2391.1000192
语种：English
出版社：OMICS International
摘要：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.
关键词：Retinoic acids; Human serum albumin; Fluorescence;Circular dichroism
