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- W2004302352 abstract "The asymmetric distribution of different lipid species in the inner and outer half of the bilayer is an important feature of many natural membranes. Certain transmembrane (TM) helix-forming peptides are known to increase the transverse diffusion (flip-flop) of lipids and can break down lipid asymmetry. We have investigated the dependence of peptide enhanced flip-flop upon TM helix sequence in order to try to understand the mechanism by which this occurs.The movement of a fluorescent phosphatidylcholine analog (6-NBD-PC) from the outer to inner leaflet was used to measure the influence of different model TM helices on the natural flip-flop rate of model membranes. The most hydrophobic TM peptides had very little or no effect upon flip-flop rate. Preliminary results indicate that for TM peptides of comparable length, a reduction of hydrophobicity increases the lipid flip-flop rate. The lipid flip-flop rate was most markedly increased when an Asp residue was introduced near the center of a highly hydrophobic sequence. The flip-flop was greatly accelerated when the Asp residue was protonated and the peptide was in a TM configuration but accelerated the most when the Asp residue was deprotonated and the peptide resided on the bilayer surface. Although certain pore forming peptides have been shown to accelerate flip-flop, no pore formation was detected for the peptides used in our studies. We conclude that perturbation of lipid packing is a possible mechanism by which hydrophobic helices accelerate flip-flop, while pore formation is unlikely to be a universal mechanism for accelerating flip-flop." @default.
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- W2004302352 date "2012-01-01" @default.
- W2004302352 modified "2023-09-29" @default.
- W2004302352 title "Effect of Hydrophobic Peptide Sequence upon Peptide-Dependent Acceleration of Lipid Flip-Flop" @default.
- W2004302352 doi "https://doi.org/10.1016/j.bpj.2011.11.464" @default.
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