Imbalance in chemical space: How to facilitate the identification of protein-protein interaction inhibitors.

ABSTRACT: Protein-protein interactions (PPIs) play vital roles in life and provide new opportunities for therapeutic interventions. In this large data analysis, 3,300 inhibitors of PPIs (iPPIs) were compared to 17 reference datasets of collectively ~566,000 compounds (including natural compounds, existing drugs, active compounds on conventional targets, etc.) using a chemoinformatics approach. Using this procedure, we showed that comparable classes of PPI targets can be formed using either the similarity of their ligands or the shared properties of their binding cavities, constituting a proof-of-concept that not only can binding pockets be used to group PPI targets, but that these pockets certainly condition the properties of their corresponding ligands. These results demonstrate that matching regio

SUBMITTER: Kuenemann MA 

PROVIDER: S-EPMC4817116 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature