Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering.
The conformation and correlations of amphiphilic and antimicrobial peptides and the associated changes of lipid bilayers can be studied in oriented lipid membranes deposited on solid substrates. Here we review recent work on these systems, as studied by modern interface-sensitive X-ray and neutron scattering methods. Density profile, short range order of acyl chains and molecular conformations of peptides and lipids are probed in the fluid state of the bilayer. With an emphasis on technical aspects, we review recent work illustrating the potential of the methods and discuss its potential in the field.
Salditt
Tim
T
Institut für Röntgenphysik, Universität Göttingen, Friedrich-Hund-Platz. 1, D-37077 Göttingen, Germany. tsaldit@gwdg.de <tsaldit@gwdg.de>
Li
Chenghao
C
Spaar
Alexander
A
D008055:Lipids / Q000737:chemistry*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012542:Scattering, Radiation; D014965:X-Rays
D008055:Lipids; D010455:Peptides