title: Understanding nature's design for a nanosyringe.
abstract: Synthetic and natural peptide assemblies can possess transport or conductance activity across biomembranes through the formation of nanopores. The fundamental mechanisms of membrane insertion necessary for antimicrobial or synthetic pore formation are poorly understood. We observe a lipid-assisted mechanism for passive insertion into a model membrane from molecular dynamics simulations. The assembly used in the study, a generic nanotube functionalized with hydrophilic termini, is assisted in crossing the membrane core by transleaflet lipid flips. Lipid tails occlude a purely hydrophobic nanotube. The observed insertion mechanism requirements for hydrophobic-hydrophilic matching have implications for the design of synthetic channels and antibiotics.
authors.affiliation: Center for Molecular Modeling, Chemistry Department, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104-6323, USA. lopez@cmm.upenn.edu
authors.forename: Carlos F
authors.initials: CF
authors.lastname: Lopez
authors.forename: Steve O
authors.initials: SO
authors.lastname: Nielsen
authors.forename: Preston B
authors.initials: PB
authors.lastname: Moore
authors.forename: Michael L
authors.initials: ML
authors.lastname: Klein
mesh_terms: D015374:Biosensing Techniques; D003198:Computer Simulation; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry*; D008567:Membranes, Artificial; D008958:Models, Molecular; D008968:Molecular Conformation
chemical_list: D008567:Membranes, Artificial; D004134:Dimyristoylphosphatidylcholine