caa a22 4500 606242899 CHVBK 20210128101321.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s12551-015-0167-5 doi (NATIONALLICENCE)springer-10.1007/s12551-015-0167-5 Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR [Elektronische Daten] [Matthieu Fillion, Michèle Auger] Overuse and misuse of antibiotics have led bacteria to acquire several mechanisms of resistance. In response to this, researchers have identified natural antimicrobial peptides as promising candidates to fight against multiresistant bacteria. However, their mode of action is still unclear, and a better understanding of the mode of action of these peptides is of primary importance to develop new peptides displaying high antibacterial activity and low hemolytic activity. One of the main features that defines the mechanism of action is the membrane topology of the peptide. Among the spectroscopic techniques, solid-state NMR is the technique of choice for determining the location of the peptide within the membrane. It can be achieved by performing experiments with oriented samples. In the literature, the two most common types of oriented samples are bicelles and phospholipids mechanically oriented between glass plates. The mode of perturbation of the membrane-active peptide can be studied by phosphorus-31 and deuterium NMR. On the other hand, several experiments such as nitrogen-15 and fluorine solid-state NMR, that require labeled peptides, can give valuable information on the membrane topology of the peptide. The combination of the latter techniques allows the determination of a precise topology, thus a better knowledge of the molecular determinants involved in the membrane interactions of antimicrobial peptides. International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg, 2015 Cationic antimicrobial peptides nationallicence Solid-state NMR nationallicence Membrane topology nationallicence Oriented samples nationallicence Model membranes nationallicence ∆χ : Magnetic susceptibility nationallicence AMP : Antimicrobial peptides nationallicence CSA : Chemical shift anisotropy nationallicence DHPC : Dihexanoylphosphatidylcholine nationallicence DMPC : Dimyristoylphosphatidylcholine nationallicence DPI : Dual polarization interferometry nationallicence NMR : Nuclear magnetic resonance nationallicence OCD : Oriented circular dichroism nationallicence PISEMA : Polarization inversion spin exchange at the magic angle nationallicence SLF : Separated-local-field nationallicence SPR : Surface plasmon resonance nationallicence Fillion Matthieu Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, G1V 0A6, Québec, QC, Canada aut Auger Michèle Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, G1V 0A6, Québec, QC, Canada aut Biophysical Reviews Springer Berlin Heidelberg 7/3(2015-09-01), 311-320 1867-2450 7:3<311 2015 7 12551 https://doi.org/10.1007/s12551-015-0167-5 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s12551-015-0167-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Fillion Matthieu Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, G1V 0A6, Québec, QC, Canada aut NATIONALLICENCE 700 1- Auger Michèle Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, G1V 0A6, Québec, QC, Canada aut NATIONALLICENCE 773 0- Biophysical Reviews Springer Berlin Heidelberg 7/3(2015-09-01), 311-320 1867-2450 7:3<311 2015 7 12551