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Non-Peptidic α-Helical Mimetics as Protein-Protein Interaction Inhibitors

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Protein-protein interactions play a major role in almost all biological pathways and thus, these interactions have a profound impact on the pathogenesis of diseases. The ability to modulate protein-protein interactions with small molecules is an important and rapidly growing area in the field of medicinal chemistry. One of the most common secondary protein structures that are involved in protein-protein interactions are α-helices. Thus, a common approach towards developing inhibitors of protein-protein interactions is to design non-peptidic small molecules that mimic the spatial orientations of the side chains of an α-helix. In this review, we will discuss a variety of small molecules including terephenyls, terephthalamides, benzamides, enaminones, benzoylureas, pyridines, imidazoles, thiazoles, pyridazines, piperazines, oxopiperazines and diphenylindanes that have been published from 2005-2010 as small molecule α- helical mimetics.

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Keywords: amphiphilic; benzamide; benzoylurea; enaminone; heterocycles; hydrogen bond; hydrophilic; non-peptidic; oxopiperazine; protein-protein interactions; pyridazine; terephenyls; terephthalamides; α-helical mimetics

Document Type: Research Article

Publication date: 2011-06-01

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
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