Scaffolds for Blocking Protein-Protein Interactions

Title: Scaffolds for Blocking Protein-Protein Interactions

Volume: 7 Issue: 10

Author(s): Stefan J. Hershberger, Song-Gil Lee and Jean Chmielewski

Affiliation:

Keywords: EVH1 domains, kinase-inducible activation domain, Calixarene Scaffolds, Quinoline-Based Scaffolds, Constrained Helices

Abstract: 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.

Cite this article as:

Hershberger J. Stefan, Lee Song-Gil and Chmielewski Jean, Scaffolds for Blocking Protein-Protein Interactions, Current Topics in Medicinal Chemistry 2007; 7 (10) . https://dx.doi.org/10.2174/156802607780906726