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In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy

Paper ID Volume ID Publish Year Pages File Format Full-Text
28582 44081 2006 5 PDF Available
Title
In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy
Abstract

In this paper, the binding of neutral red (NR) to bovine serum albumin (BSA) under physiological conditions has been studied by spectroscopy method including fluorescence, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy. The Stern–Volmer fluorescence quenching constant (KSV), binding constant (Kb) and the number of binding sites (n) were measured by fluorescence quenching method. Fluorescence experiments were also performed at different ionic strengths. It was found KSV was ionic strength dependent, which indicated the electrostatic interactions were part of the binding forces. The distance r between donor (BSA) and acceptor (NR) was obtained according to Foster's non-radiative energy transfer theory. CD spectroscopy and FT-IR spectroscopy were used to investigate the structural information of BSA molecules on the binding of NR, and the results showed no change of BSA conformation in our experimental conditions.

Keywords
Neutral red; Bovine serum albumin; Molecular spectroscopy
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In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 184, Issues 1–2, 15 November 2006, Pages 93–97
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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