Summary
Protein–protein interactions are ubiquitous, essential to almost all known biological processes, and offer attractive opportunities for therapeutic intervention. Develo** small molecules that modulate protein–protein interactions is challenging, owing to the large size of protein-complex interface, the lack of well-defined binding pockets, etc. We describe a general approach based on the “privileged-structure hypothesis” [Che, Ph.D. Thesis, Washington University, 2003] – that any organic templates capable of mimicking surfaces of protein-recognition motifs are potential privileged scaffolds as protein-complex antagonists – to address the challenges inherent in the discovery of small-molecule inhibitors of protein–protein interactions.
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Acknowledgement
This research was supported in part by the Intramural Research Program of the NIH, NHLBI (BRB) and an NIH research grant (GM 68460) to GRM. Y.C. also acknowledges graduate support from the Division of Biology and Biomedical Science of Washington University in St Louis and a postdoctoral fellowship from the National Heart, Lung and Blood Institute. This work is taken in part from his Ph.D. thesis in Molecular Biophysics.
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This paper is adapted from a presentation at the 230th National Meeting of the American Chemical Society, Washington DC, August 28 – September 1, 2005, Abstract COMP-136.
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Che, Y., Brooks, B.R. & Marshall, G.R. Development of small molecules designed to modulate protein–protein interactions. J Comput Aided Mol Des 20, 109–130 (2006). https://doi.org/10.1007/s10822-006-9040-8
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DOI: https://doi.org/10.1007/s10822-006-9040-8