title: Progression of NMR studies of membrane-active peptides from lipid bilayers to live cells.
abstract: Understanding the structure of membrane-active peptides faces many challenges associated with the development of appropriate model membrane systems as the peptide structure depends strongly on the lipid environment. This perspective provides a brief overview of the approach taken to study antimicrobial and amyloid peptides in phospholipid bilayers using oriented bilayers and magic angle spinning techniques. In particular, Boltzmann statistics REDOR and maximum entropy analysis of spinning side bands are used to analyse systems where multiple states of peptide or lipid molecules may co-exist. We propose that in future, rather than model membranes, structural studies in whole cells are feasible.
authors: School of Chemistry, Bio21 Institute, University of Melbourne, VIC 3010, Australia.
authors: M-A
authors: MA
authors: Sani
authors: School of Chemistry, Bio21 Institute, University of Melbourne, VIC 3010, Australia. Electronic address: fs@unimelb.edu.au.
authors: F
authors: F
authors: Separovic
mesh_terms: D000465:Algorithms; D001665:Binding Sites; D002462:Cell Membrane / Q000737:chemistry* / Q000648:ultrastructure*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins
keywords: Amyloid peptides; Antimicrobial peptides; Lipid–peptide interactions; MAS; Oriented bilayers; Phospholipid bilayers; REDOR; Solid-state NMR