Conformations and Dynamic Transitions of a Melittin Derivative That Forms Macromolecule-Sized Pores in Lipid Bilayers
| Autor: | Brendan P. Marsh, Gavin M. King, Anna E. Pittman |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Lipid Bilayers Molecular Conformation Peptide 010402 general chemistry 01 natural sciences Melittin 03 medical and health sciences chemistry.chemical_compound Electrochemistry General Materials Science Lipid bilayer POPC Spectroscopy chemistry.chemical_classification Chemistry Bilayer Surfaces and Interfaces Condensed Matter Physics Melitten 0104 chemical sciences 030104 developmental biology Membrane Biophysics lipids (amino acids peptides and proteins) Peptides Derivative (chemistry) Macromolecule |
| Zdroj: | Langmuir. 34:8393-8399 |
| ISSN: | 1520-5827 0743-7463 |
| DOI: | 10.1021/acs.langmuir.8b00804 |
| Popis: | Systematically evolved from the primary active component of bee venom, MelP5 is a lipophilic peptide with important physical properties that differ from wild-type melittin, including the ability to create large equilibrium pores in lipid bilayers at low peptide to lipid ratios. Self-assembly into stable membrane spanning pores makes MelP5 a promising candidate for future applications in the pharmaceutical arena. Despite significant interest, little is known about the mechanism by which MelP5 remodels the lipid bilayer upon binding. We demonstrate by direct atomic force microscope imaging of supported lipid bilayers in solution that MelP5 remodels 1-palmitoyl-2-oleoyl- sn-glycero-3-phosphocholine (POPC) in one of two ways. It creates either highly localized voids in the bilayer or diffuse nonlocalized thinning. Thinning of the bilayer was measured to be 3.0 ± 1.4 Å (mean ± standard deviation) below the surface of the upper leaflet of the bilayer. Pores, defined as highly localized voids in the bilayer, exhibited several sizes. Approximately 20% of pores exhibited large footprint areas (47 ± 20 nm |
| Databáze: | OpenAIRE |
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