Dresden 2020 – scientific programme

The DPG Spring Meeting in Dresden had to be cancelled! Read more ...

Parts | Days | Selection | Search | Updates | Downloads | Help

CPP: Fachverband Chemische Physik und Polymerphysik

CPP 2: Focus: Soft Matter and Nanocomposites - New opportunities with advanced neutron sources I

CPP 2.9: Invited Talk

Monday, March 16, 2020, 12:15–12:45, ZEU 222

Antimicrobial peptides, their mechanisms of action and self- assembly revealed by scattering techniques — Josefine Eilsø Nielsen, Nico König, and •Reidar Lund — Department of Chemistry, University of Oslo, Norway

Antimicrobial peptides are remarkably effective towards a broad spec trum of bacteria and seem to be able to evade much of the resis- tance mechanisms making their interesting as therapeutics. Their main mode-of action is believed to be through selective interactions with the cytoplasmic membrane, although the microscopic mechanisms is not yet fully understood. Unfortunately, these compounds cannot easily be translated into medical applications due to degradation and hemolysis. However, self-assembly might be a promising strategy to improve the stability. First, we will consider natural antimicrobial peptides and their interactions with model lipid membranes mimicking mammalian and bacterial cells. Using Small-angle X-ray (SAXS) and neutron reflectometry, we extract the location of the peptide and the structure of the lipid bilayer. The lipid dynamics, i.e. flip-flop and molecular exchange, can be deducted using time-resolved SANS . Comparing the structure and the dynamics, we obtain unique microscopic insight into the mode-of-action. In the last part, we present results of a series of de novo designed antimicrobial peptide that assemble into nanosheet- like structures with enhanced in vivo stability. Using results various neutron scattering techniques, we will discuss the 2D/3D assembly, interfacial interactions and dynamic stability of these compounds.