AI Article Synopsis
- The study examines how melittin, a peptide, interacts with different lipid structures like liposomes, bilayer disks, and micelles, finding that its binding is influenced by the curvature of these structures.
- Characterization methods such as small angle neutron scattering and cryo-transmission electron microscopy confirm key structural properties of PEG-stabilized bilayer disks, including lipid segregation crucial for their stability.
- The research suggests that bilayer disks may serve as effective carriers for peptides like melittin, which prefer to bind to lipid surfaces that are highly curved.
Article Abstract
Comparison of melittin interaction with liposomes, bilayer disks and micelles showed that melittin binding to lipid aggregates is largely dictated by the amount of highly curved areas in the aggregates. The PEG-stabilised bilayer disks were characterised by a combination of small angle neutron scattering, cryo-transmission electron microscopy and dynamic light scattering. Importantly, the theoretically foreseen partial segregation of the lipid components, important for maintaining the structure of the bilayer disk, was confirmed. Steady state fluorescence spectroscopy indicated that melittin mainly resides at the rim of the bilayer disks. Results of the present study help increase the understanding of the mechanisms behind, and the physico-chemical factors affecting, melittin-lipid interaction. We suggest that bilayer disks, due to their stable structure, constitute interesting vehicles for transport of peptides that have high propensity to associate with lipid surfaces of high curvature.
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| http://dx.doi.org/10.1016/j.bbamem.2008.05.009 | DOI Listing |
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