title: Anisotropic Membrane Curvature Sensing by Amphipathic Peptides.
abstract: Many proteins and peptides have an intrinsic capacity to sense and induce membrane curvature, and play crucial roles for organizing and remodeling cell membranes. However, the molecular driving forces behind these processes are not well understood. Here, we describe an approach to study curvature sensing by simulating the interactions of single molecules with a buckled lipid bilayer. We analyze three amphipathic antimicrobial peptides, a class of membrane-associated molecules that specifically target and destabilize bacterial membranes, and find qualitatively different sensing characteristics that would be difficult to resolve with other methods. Our findings provide evidence for direction-dependent curvature sensing mechanisms in amphipathic peptides and challenge existing theories of hydrophobic insertion. The buckling approach is generally applicable to a wide range of curvature-sensing molecules, and our results provide strong motivation to develop new experimental methods to track position and orientation of membrane proteins.
authors.affiliation: Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. Electronic address: jgomez@turbula.es.
authors.forename: Jordi
authors.initials: J
authors.lastname: Gómez-Llobregat
authors.affiliation: Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. Electronic address: federico.elias.wolff@dbb.su.se.
authors.forename: Federico
authors.initials: F
authors.lastname: Elías-Wolff
authors.affiliation: Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden. Electronic address: martin.linden@icm.uu.se.
authors.forename: Martin
authors.initials: M
authors.lastname: Lindén
mesh_terms: D016880:Anisotropy; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism*; D001696:Biomechanical Phenomena; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D056004:Molecular Dynamics Simulation; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D023181:Antimicrobial Cationic Peptides