Structure-Activity Relationships of the Antimicrobial Peptide Natural Product Apidaecin.

ABSTRACT: With the growing crisis of antimicrobial resistance, it is critical to continue to seek out new sources of novel antibiotics. This need has led to renewed interest in natural product antimicrobials, specifically antimicrobial peptides. Nonlytic antimicrobial peptides are highly promising due to their unique mechanisms of action. One such peptide is apidaecin (Api), which inhibits translation termination through stabilization of the quaternary complex of the ribosome-apidaecin-tRNA-release factor. Synthetic derivatives of apidaecin have been developed, but structure-guided modifications have yet to be considered. In this work, we have focused on modifying key residues in the Api sequence that are responsible for the interactions that stabilize the quaternary complex. We present one of the f

SUBMITTER: Skowron KJ 

PROVIDER: S-EPMC10768847 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature