Novel Helical Trp- and Arg-Rich Antimicrobial Peptides Locate Near Membrane Surfaces and Rigidify Lipid Model Membranes.

ABSTRACT: Antibiotics are losing effectiveness as bacteria become resistant to conventional drugs. To find new alternatives, antimicrobial peptides (AMPs) are rationally designed with different lengths, charges, hydrophobicities (H), and hydrophobic moments (μH), containing only three types of amino acids: arginine, tryptophan, and valine. Six AMPs with low minimum inhibitory concentrations (MICs) and <25% toxicity to mammalian cells are selected for biophysical studies. Their secondary structures are determined using circular dichroism (CD), which finds that the % α-helicity of AMPs depends on composition of the lipid model membranes (LMMs): gram-negative (G(-)) inner membrane (IM) >gram-positive (G(+)) > Euk33 (eukaryotic with 33 mol% cholesterol). The two most effective peptides, E2-35 (16 amino

SUBMITTER: Mitra S 

PROVIDER: S-EPMC10358585 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature