Stefan J. Hershberger, Song-Gil Lee and Jean Chmielewski Pages 928 - 942 ( 15 )
Due to the pivotal roles that protein-protein interactions play in a plethora of biological processes, the design of therapeutic agents targeting these interactions has become an attractive and important area of research. The development of such agents is faced with a variety of challenges. Nevertheless, considerable progress has been made in the design of proteomimetics capable of disrupting proteinprotein interactions. Those inhibitors based on molecular scaffold designs hold considerable interest because of the ease of variation in regard to their displayed functionality. In particular, protein surface mimetics, α-helical mimetics, β-sheet/β-strand mimetics, as well as β- turn mimetics have successfully modulated protein-protein interactions involved in such diseases as cancer and HIV. In this review, current progress in the development of molecular scaffolds designed for the disruption of protein-protein interactions will be discussed with an emphasis on those active against biological targets.
EVH1 domains, kinase-inducible activation domain, Calixarene Scaffolds, Quinoline-Based Scaffolds, Constrained Helices
Department of Chemistry,Purdue University, West Lafayette, Indiana, 47907, USA.