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The interaction of C.I. acid red 27 with human hemoglobin in solution

Paper ID Volume ID Publish Year Pages File Format Full-Text
31045 44533 2010 8 PDF Available
Title
The interaction of C.I. acid red 27 with human hemoglobin in solution
Abstract

The nature of the interaction between human hemoglobin and C.I. acid red 27 was investigated systematically by ultraviolet–vis absorbance, circular dichroism, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques at pH 7.40. The quenching mechanism, binding constants, and the number of binding sites were determined by the quenching of human hemoglobin fluorescence in presence of C.I. acid red 27. The results showed that the nature of the quenching was of static type and the process of binding acid red 27 on human hemoglobin was a spontaneous molecular interaction procedure. The electrostatic and hydrophobic interactions played a major role in stabilizing the complex; The distance r between donor and acceptor was obtained to be 4.40 nm according to Förster’s theory; The effect of acid red 27 on the conformation of human hemoglobin was analyzed using synchronous fluorescence, circular dichroism and three-dimensional fluorescence spectra.

Keywords
Acid red 27; Human hemoglobin; Fluorescence study; Interaction with protein; Thermodynamic parameters; Three-dimensional fluorescence spectra
First Page Preview
The interaction of C.I. acid red 27 with human hemoglobin in solution
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 100, Issue 2, 2 August 2010, Pages 76–83
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering