Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly.

ABSTRACT: Antimicrobial peptides (AMPs) are ubiquitous weapons of all higher organisms to suppress antimicrobial growth. Despite intensive research, the killing mechanism of these peptides after interaction with the bacterial cell wall and cytoplasm is not well understood. To investigate this mechanism at a molecular level, we chose a well-studied AMP, Magainin-2 (Mag-2), for biophysical and structural studies. Circular dichroism experiments showed that the folding propensity of Mag-2 is strongly altered towards fully folded molecules in the presence of detergent. To study the pore-forming properties of Mag-2 in membranes, we crystallized the wild-type peptide in the presence of the membrane-mimicking dodecylphosphocholine detergent and obtained crystals diffracting to atomic resolution. Mag-2 struc

SUBMITTER: Sancho-Vaello E 

PROVIDER: S-EPMC12615594 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature