Understanding nature's design for a nanosyringe.

Lopez CF, Nielsen SO, Moore PB, Klein ML
Proc Natl Acad Sci U S A. 2004 101 (13): 4431-4

PMID: 15070735 · PMCID: PMC384764 · DOI:10.1073/pnas.0400352101

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.

MeSH Terms (6)

Biosensing Techniques Computer Simulation Dimyristoylphosphatidylcholine Membranes, Artificial Models, Molecular Molecular Conformation

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