Investigation of binding properties of dicationic styrylimidazo[1,2-a]pyridinium dyes to human serum albumin by spectroscopic techniques

Date
2017
Advisor
Instructor
Source Title
Luminescence
Print ISSN
1522-7235
Electronic ISSN
Publisher
John Wiley and Sons Ltd
Volume
32
Issue
1
Pages
86 - 92
Language
English
Type
Article
Journal Title
Journal ISSN
Volume Title
Abstract

The binding interaction between two dicationic styrylimidazo[1,2-a]pyridinium dyes and human serum albumin (HSA) was investigated at physiological conditions using fluorescence, UV–vis absorption, and circular dichroism (CD) spectroscopies. Analysis of the fluorescence titration data at different temperatures suggested that the fluorescence quenching mechanism of HSA by these dyes was static. The calculated thermodynamic parameters (ΔG°, ΔH° and ΔS°) indicated that hydrogen bonding and van der Waals forces played a major role in the formation of the dye–HSA complex. Binding distances (r) between dyes and HSA were calculated according to Förster's non-radiative energy transfer theory. Studies of conformational changes of HSA using CD measurements indicate that the α-helical content of the protein decreased upon binding of the dyes.

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Keywords
Binding mode, Circular dichroism, Dicationic styryl dyes, Fluorescence quenching, Human serum albumin, Cation, Fluorescent dye, Imidazole derivative, Pyridinium derivative, Serum albumin, Styrylimidazo(1,2-a)pyridinium, Binding site, Chemistry, Circular dichroism, Human, Spectrofluorometry, Thermodynamics, Ultraviolet spectrophotometry, Binding Sites, Cations, Circular Dichroism, Fluorescent Dyes, Imidazoles, Pyridinium Compounds, Serum Albumin, Spectrometry, Spectrophotometry, Thermodynamics, Ultraviolet, Fluorescence
Citation
Published Version (Please cite this version)