Abstract

Peptide Toxins Venomous animals typically produce peptides and proteins that have potent biological activities through their interaction with membranes or cellular targets. Silva et al. analyzed the sequence and structure of a short peptide toxin from the wasp Vespula lewisii and reengineered it into an antimicrobial peptide. Modifications to the end of the peptide reduced toxicity to mammalian cells while preserving the ability to disrupt the outer membrane of Gram-negative bacteria. Antimicrobial activity in mouse infection models demonstrated promising potential for the original design and various analogs. Proc. Natl. Acad. Sci. U.S.A. 117 , 26936 (2020).

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call