Solid-phase synthesis and screening of N-acylated polyamine (NAPA) combinatorial libraries for protein binding.

ABSTRACT: Inhibitors for protein-protein interactions are challenging to design, in part due to the unique and complex architectures of each protein's interaction domain. Most approaches to develop inhibitors for these interactions rely on rational design, which requires prior structural knowledge of the target and its ligands. In the absence of structural information, a combinatorial approach may be the best alternative to finding inhibitors of a protein-protein interaction. Current chemical libraries, however, consist mostly of molecules designed to inhibit enzymes. In this manuscript, we report the synthesis and screening of a library based on an N-acylated polyamine (NAPA) scaffold that we designed to have specific molecular features necessary to inhibit protein-protein interactions. Screens of

SUBMITTER: Iera JA 

PROVIDER: S-EPMC2982675 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature