Investigation of the Role of Hydrophobic Amino Acids on the Structure-Activity Relationship in the Antimicrobial Venom Peptide Ponericin L1.

ABSTRACT: Venom mixtures from insects, reptiles, and mollusks have long been a source of bioactive peptides which often have alternative uses as therapeutics. While these molecules act in numerous capacities, there have been many venom components that act on the target cells through membrane disruptive mechanisms. These peptides have long been of interest as potential antimicrobial peptide platforms, but the inherent cytotoxicity of venom peptides often results in poor therapeutic potential. Despite this, efforts are ongoing to identify and characterize venom peptide which exhibit high antimicrobial activity with low cytotoxicity and modify these to further enhance the efficacy while reducing toxicity. One example is ponericin L1 from Neoponera goeldii which has been demonstrated to have good antimi

SUBMITTER: Schifano NP 

PROVIDER: S-EPMC9114170 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature