Zsila Ferenc, Bikádi Zsolt, Fitos Ilona, Simonyi Miklós
Department of Molecular Pharmacology, Institute of Chemistry, Chemical Research Centre, Budapest, POB 17, 1525, Hungary.
Curr Drug Discov Technol. 2004 Jun;1(2):133-53. doi: 10.2174/1570163043335135.
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.
生物活性天然和合成化合物的药理及药效学特性主要通过它们与人体蛋白质的结合来关键地确定。有几种光谱技术可用于研究这些主要是非共价相互作用。圆二色（CD）光谱对由不对称蛋白质环境诱导的配体分子的手性敏感，几十年来已被广泛且成功地应用。由于配体构象适应其结合位点，或者由蛋白质位点使配体分子以手性排列相互保持的分子间相互作用，导致出现一个或多个具有不同形状、符号和强度的诱导CD带。这些存在于光学活性或非活性配体分子光吸收区域的外在科顿效应给出了结合过程的定性和定量信息。它可以提供关于结合位点的立体化学、数量、位置和性质的有价值数据。本文旨在简要综述该领域的文献和近期研究结果。
