Identification of protease exosite-interacting peptides that enhance substrate cleavage kinetics.

ABSTRACT: Many peptidases are thought to require non-active site interaction surfaces, or exosites, to recognize and cleave physiological substrates with high specificity and catalytic efficiency. However, the existence and function of protease exosites remain obscure owing to a lack of effective methods to identify and characterize exosite-interacting substrates. To address this need, we modified the cellular libraries of peptide substrates (CLiPS) methodology to enable the discovery of exosite-interacting peptide ligands. Invariant cleavage motifs recognized by the active sites of thrombin and caspase-7 were displayed on the outer surface of bacteria adjacent to a candidate exosite-interacting peptide. Exosite peptide libraries were then screened for ligands that accelerate cleavage of the active

SUBMITTER: Jabaiah AM 

PROVIDER: S-EPMC3858821 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature