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Single-Molecule Resolution of Antimicrobial Peptide Interactions with Supported Lipid A Bilayers by Nathaniel Nelson; Daniel K. Schwartz is a scholarly article available to read on EtoBox.

What is Single-Molecule Resolution of Antimicrobial Peptide Interactions with Supported Lipid A Bilayers about?

The molecular interactions between antimicrobial peptides (AMPs) and lipid A-containing supported lipid bilayers were probed using single-molecule total internal reflection fluorescence microscopy. Hybrid supported lipid bilayers with lipid A outer leaflets and phospholipid (1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE)) inner leaflets were prepared and characterized, and the spatiotemporal trajectories of individual fluorescently labeled LL37 and Melittin AMPs were determined as they interacted with the bilayer surfaces comprising either monophosphoryl or diphosphoryl lipid A (from Escherichia coli) to determine the impact of electrostatic interactions. Large numbers of trajectories were obtained and analyzed to obtain the distributions of surface residence times and the statistics of the spatial trajectories. Interestingly, the AMP species were sensitive to subtle differences in the charge of the lipid, with both peptides diffusing more slowly and residing longer on the diphosphoryl lipid A. Furthermore, the single-molecule dynamics indicated a qualitative difference between the behavior of AMPs on hybrid Lipid A bilayers and on those composed entirely of DOPE. Whereas AMP

Author

Nathaniel Nelson; Daniel K. Schwartz

Publisher

Biophysical Society; Elsevier ; Elsevier BV (ISSN 0006-3495)

Published

2018

Language

EN