Two distinct amphipathic peptide antibiotics with systemic efficacy.

ABSTRACT: Antimicrobial peptides are important candidates for developing new classes of antibiotics because of their potency against antibiotic-resistant pathogens. Current research focuses on topical applications and it is unclear how to design peptides with systemic efficacy. To address this problem, we designed two potent peptides by combining database-guided discovery with structure-based design. When bound to membranes, these two short peptides with an identical amino acid composition can adopt two distinct amphipathic structures: A classic horizontal helix (horine) and a novel vertical spiral structure (verine). Their horizontal and vertical orientations on membranes were determined by solid-state ¹⁵N NMR data. While horine was potent primarily against gram-positive pathogens, verin

SUBMITTER: Lakshmaiah Narayana J 

PROVIDER: S-EPMC7431008 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature