Antibiotic Potential and Biophysical Characterization of Amphipathic β-Stranded [XZ]_n Peptides With Alternating Cationic and Hydrophobic Residues.

ABSTRACT: Cationic membrane-active peptides are considered to be promising candidates for antibiotic treatment. Many natural and artificial sequences show an antimicrobial activity when they are able to take on an amphipathic fold upon membrane binding, which in turn perturbs the integrity of the lipid bilayer. Most known structures are α-helices and β-hairpins, but also cyclic knots and other irregular conformations are known. Linear β-stranded antimicrobial peptides are not so common in nature, but numerous model sequences have been designed. Interestingly, many of them tend to be highly membranolytic, but also have a significant tendency to self-assemble into β-sheets by hydrogen-bonding. In this minireview we examine the literature on such amphipathic peptides consisting of simple repetitive seq

SUBMITTER: Strandberg E 

PROVIDER: S-EPMC8757834 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature