Sezgin Kara

TL;DR: The absence of a typical thinning response in the case of PGLa, and the increase in the repeat distance and membrane thickening observed for TisB, demonstrate that the concept of peptide-induced membrane thinning cannot be generalized and suggest that different factors contribute to the resulting changes in membrane thickness.

TL;DR: The exchange of native proline for γ-trifluoromethyl proline in the peptide antibiotic gramicidin S was shown to preserve the overall amphipathic peptide structure and the utility of the amino acid as a selective (19)F-NMR label was demonstrated.

TL;DR: It was found that the α-helical PGLa was not able to insert into the tightly packed fluid bilayer of DPhPC but remained in a surface-bound state even at very high peptide concentration, which can be explained by the high cohesivity and the negative spontaneous curvature of the diphytanoyl lipids.

TL;DR: Overall, these results confirm the functional isosterism of Nle and Met in the helical membrane-active peptides but highlight differences in the ways in which the two residues affect non-specific binding to the lipid bilayer and homomeric peptide-peptide interactions.

TL;DR: For the short sequence of 11 amino acids, 12 orientational constraints have been obtained by using 19 F and 15 N NMR spectroscopy and revealed a β-bend ribbon structure, which becomes realigned in the membrane from a surface-parallel state towards a membrane-spanning state, with increasing positive spontaneous curvature of the lipids.