Eichler Jutta
Department Medicinal Chemistry, University of Erlangen-Nuremberg, Schuhstrasse 19, 91052 Erlangen, Germany.
Curr Opin Chem Biol. 2008 Dec;12(6):707-13. doi: 10.1016/j.cbpa.2008.09.023. Epub 2008 Oct 18.
The rational/structure-based design and/or combinatorial development of molecules capable of structurally and functionally mimicking the binding sites of proteins represents a promising strategy for the exploration and understanding of protein structure and function. The ultimate goal of using such molecules is the modulation of protein function through controlled interference with the underlying binding events. In addition to their basic significance, such proteinmimetics are also useful tools for a range of biomedical applications, in particular the inhibition of disease-associated protein-ligand interactions. Owing to their chemical and structural relation to proteins, as well as the relative simplicity of their chemical or recombinant synthesis, peptides have emerged as adequate molecules for the mimicry of protein binding sites, as well as the inhibition of protein-protein interactions.
基于理性/结构的设计和/或组合开发能够在结构和功能上模拟蛋白质结合位点的分子，是探索和理解蛋白质结构与功能的一种有前景的策略。使用这类分子的最终目标是通过对潜在结合事件的可控干扰来调节蛋白质功能。除了其基本意义外，这类蛋白质模拟物也是一系列生物医学应用的有用工具，特别是抑制与疾病相关的蛋白质-配体相互作用。由于其与蛋白质的化学和结构关系，以及化学或重组合成相对简单，肽已成为模拟蛋白质结合位点以及抑制蛋白质-蛋白质相互作用的合适分子。
