Physicochemical-guided design of cathelicidin-derived peptides generates membrane active variants with therapeutic potential.

ABSTRACT: The spread of multi-drug resistance and the slow pace at which antibiotics come onto the market are undermining our ability to treat human infections, leading to high mortality rates. Aiming to overcome this global crisis, antimicrobial peptides are considered promising alternatives to counter bacterial infections with multi-drug resistant bacteria. The cathelicidins comprise a well-studied class of AMPs whose members have been used as model molecules for sequence modifications, aiming at enhanced biological activities and stability, along with reduced toxic effects on mammalian cells. Here, we describe the antimicrobial activities, modes of action and structural characterization of two novel cathelicidin-like peptides, named BotrAMP14 and CrotAMP14, which were re-designed from snake batro

SUBMITTER: Oliveira NGJ 

PROVIDER: S-EPMC7272458 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature