Abstract
Pharmacological and pharmacodynamic properties of biologically active natural and synthetic compounds are crucially determined via their binding to proteins of the human body. Several spectroscopic techniques are available to study these mainly non-covalent interactions. Circular dichroism (CD) spectroscopy, being sensitive to the chirality of ligand molecules induced by the asymmetric protein environment, has widely and successfully been applied for many decades. Chiral conformation of the ligand due to conformational adaptation to its binding site, or interaction between ligand molecules held in chiral arrangement relative to each other by the protein sites, results in one or more induced CD bands with different shape, sign and intensity. These extrinsic Cotton effects present in light absorbing region of the optically active or inactive ligand molecules give qualitative and quantitative information of the binding process. It can provide valuable data on the stereochemistry, number, location and nature of the binding sites. This paper is aimed to survey briefly the literature and the results of recent investigations undertaken in this field.
Keywords: Circular dichroism spectroscopy, Chiral conformation, Exciton coupling, Extrinsic Cotton effects
Current Drug Discovery Technologies
Title: Probing Protein Binding Sites by Circular Dichroism Spectroscopy
Volume: 1 Issue: 2
Author(s): Ferenc Zsila, Zsolt Bikadi, Ilona Fitos and Miklos Simonyi
Affiliation:
Keywords: Circular dichroism spectroscopy, Chiral conformation, Exciton coupling, Extrinsic Cotton effects
Abstract: Pharmacological and pharmacodynamic properties of biologically active natural and synthetic compounds are crucially determined via their binding to proteins of the human body. Several spectroscopic techniques are available to study these mainly non-covalent interactions. Circular dichroism (CD) spectroscopy, being sensitive to the chirality of ligand molecules induced by the asymmetric protein environment, has widely and successfully been applied for many decades. Chiral conformation of the ligand due to conformational adaptation to its binding site, or interaction between ligand molecules held in chiral arrangement relative to each other by the protein sites, results in one or more induced CD bands with different shape, sign and intensity. These extrinsic Cotton effects present in light absorbing region of the optically active or inactive ligand molecules give qualitative and quantitative information of the binding process. It can provide valuable data on the stereochemistry, number, location and nature of the binding sites. This paper is aimed to survey briefly the literature and the results of recent investigations undertaken in this field.
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Cite this article as:
Zsila Ferenc, Bikadi Zsolt, Fitos Ilona and Simonyi Miklos, Probing Protein Binding Sites by Circular Dichroism Spectroscopy, Current Drug Discovery Technologies 2004; 1 (2) . https://dx.doi.org/10.2174/1570163043335135
DOI https://dx.doi.org/10.2174/1570163043335135 |
Print ISSN 1570-1638 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6220 |
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