HIV Fusion Peptides Significantly Soften Lipid Bilayers

Cell-penetrating HIV1 TAT peptides float on model lipid bilayers.

Cell-penetrating peptides like the cationic HIV1 TAT peptide are able to translocate across cell membranes and to carry molecular cargoes into the cellular interior. For most of these peptides, the biophysical mechanism of the membrane translocation is still quite unknown. We analyzed HIV1 TAT peptide binding and mobility within biological model membranes. To this end, we generated neutral and ...

Infrared spectroscopy of proteins and peptides in lipid bilayers.

Simulation of fusion-mediated nanoemulsion interactions with model lipid bilayers.

Perfluorocarbon-based nanoemulsion particles have become promising platforms for the delivery of therapeutic and diagnostic agents to specific target cells in a non-invasive manner. A "contact-facilitated" delivery mechanism has been proposed wherein the emulsifying phospholipid monolayer on the nanoemulsion surface contacts and forms a lipid complex with the outer monolayer of target cell plas...

Formation of nanopore-spanning lipid bilayers through liposome fusion.

Self-assembly of nanopore-spanning lipid bilayers (npsLBs) paves the way toward chip-based integrated membrane protein biosensing. We present a novel approach to analyze the formation of npsLB at individual nanopores using quantitative analysis of high-resolution microscopy images. From this analysis we derive necessary conditions for the formation of npsLBs on nanopore arrays by liposome fusio...

Secretory and viral fusion may share mechanistic events with fusion between curved lipid bilayers.

Activation energies for the individual steps of secretory and viral fusion are reported to be large [Oberhauser, A. F., Monck, J. R. & Fernandez, J. M. (1992) Biophys. J. 61, 800-809; Clague, M. J., Schoch, C., Zech, L. & Blumenthal, R. (1990) Biochemistry 29, 1303-1308]. Understanding the cause for these large activation energies is crucial to defining the mechanisms of these two types of biol...