Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities.

ABSTRACT: Frogs such as Rana temporaria and Litoria aurea secrete numerous closely related antimicrobial peptides (AMPs) as an effective chemical dermal defence. Damage or penetration of the bacterial plasma membrane is considered essential for AMP activity and such properties are commonly ascribed to their ability to form secondary amphipathic, α-helix conformations in membrane mimicking milieu. Nevertheless, despite the high similarity in physical properties and preference for adopting such conformations, the spectrum of activity and potency of AMPs often varies considerably. Hence distinguishing apparently similar AMPs according to their behaviour in, and effects on, model membranes will inform understanding of primary-sequence-specific antimicrobial mechanisms. Here we use a combination of molec

SUBMITTER: Manzo G 

PROVIDER: S-EPMC6662694 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature