Scientists from IBCh RAS and colleagues clarify the structural basis of thanatin-like antimicrobial peptide activity
Scientists from IBCh RAS and their colleagues investigated Rip-2, a natural thanatin-like antimicrobial peptide from the bean bug Riptortus pedestris, and found that its enhanced activity may depend on its C-terminal phenylalanine residue. Selection of E. coli clones with reduced Rip-2 susceptibility identified an R76C substitution in LptA, a component of the lipopolysaccharide transport system. Peptide mutagenesis, analysis of natural homologs, and structure-guided modeling allowed the authors to propose a testable model in which Rip-2 Phe18 contributes to LptA-dependent target engagement. The study clarifies the mechanism of action of thanatin-like peptides and may guide the rational design of new antibiotics. Learn more
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