14 March 2014

First High-Resolution Structures of Antimicrobial Peptides Reveal Important Structural Features

Structures of antimicrobial peptides piscidins 1 and 3 were solved in two bacterial cell mimics by oriented sample solid-state NMR. A significant finding of this work is that in contrast to the ideal structures shown in mechanistic studies of AMPs, the structures of both peptides are disrupted and kinked at a conserved central glycine, which results in stronger interactions with the lipid bilayers. The more pronounced imperfect amphipathicity of piscidin 1 over piscidin 3 that is revealed helps better understand why the former more effectively mixes the lipids as needed to induce the greatest damage to bacterial cells.

For more information contact Tim Cross, This email address is being protected from spambots. You need JavaScript enabled to view it..

Details

  • Research Area: Biochemistry
  • Research Initiatives: Life
  • Facility / Program: NMR/MRI
  • Year: 2014
Last modified on 17 April 2015