1 research outputs found
Peptides at the Interface: Self-Assembly of Amphiphilic Designer Peptides and Their Membrane Interaction Propensity
Self-assembling
amphiphilic designer peptides have been successfully
applied as nanomaterials in biomedical applications. Understanding
molecular interactions at the peptide–membrane interface is
crucial, since interactions at this site often determine (in)Âcompatibility.
The present study aims to elucidate how model membrane systems of
different complexity (in particular single-component phospholipid
bilayers and lipoproteins) respond to the presence of amphiphilic
designer peptides. We focused on two short anionic peptides, V<sub>4</sub>WD<sub>2</sub> and A<sub>6</sub>YD, which are structurally
similar but showed a different self-assembly behavior. A<sub>6</sub>YD self-assembled into high aspect ratio nanofibers at low peptide
concentrations, as evidenced by synchrotron small-angle X-ray scattering
and electron microscopy. These supramolecular assemblies coexisted
with membranes without remarkable interference. In contrast, V<sub>4</sub>WD<sub>2</sub> formed only loosely associated assemblies over
a large concentration regime, and the peptide promoted concentration-dependent
disorder on the membrane arrangement. Perturbation effects were observed
on both membrane systems although most likely induced by different
modes of action. These results suggest that membrane activity critically
depends on the peptide’s inherent ability to form highly cohesive
supramolecular structures