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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.

SUBMITTER: Lopez CF

PROVIDER: S-EPMC384764 | biostudies-literature | 2004 Mar

REPOSITORIES: biostudies-literature

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Understanding nature's design for a nanosyringe.

Lopez Carlos F CF Nielsen Steve O SO Moore Preston B PB Klein Michael L ML

Proceedings of the National Academy of Sciences of the United States of America 20040312 13

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 cro ...[more]

PMID: 15070735

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Dataset Information

Understanding nature's design for a nanosyringe.

Publications

Understanding nature's design for a nanosyringe.

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