Publication | Closed Access
Shape Changes of Giant Unilamellar Vesicles of Phosphatidylcholine Induced by a De Novo Designed Peptide Interacting with Their Membrane Interface
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Citations
13
References
2002
Year
Membrane StructureProteinlipid InteractionPeptide SciencePeptide TherapeuticsAnalytical UltracentrifugationLipid MovementSmall VesiclesPhosphatidylcholine InducedProtein FoldingBiophysicsBiochemistryPeptide-1 ConcentrationMembrane BiologyMembrane SystemLipopeptidesBiomolecular EngineeringMembrane BiophysicsNatural SciencesPc Membrane InterfaceShape ChangesMedicineGiant Unilamellar Vesicles
We have designed and synthesized a peptide, WLFLLKKK (peptide-1), which has positive charges and a segment partitioned into the electrically neutral lipid membrane interface, and investigated its effect on the stability of the phosphatidylcholine (PC) membrane. Spacing of multilamellar vesicles of palmitoyloleoyl-PC increased greatly with an increase in peptide-1 concentration. The addition of 5 μM peptide-1 through a micropipet near the giant unilamellar vesicle (GUV) of dioleoylphosphatidylcholine induced several kinds of shape changes; for example, a discocyte was changed to two spheres connected by a neck, and small vesicles were budded into the outside of the spherical GUV. These results indicate that the de novo designed peptide-1 can be partitioned into the PC membrane interface and have a large effect on its structure and properties.
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