Secondary structure in de novo designed peptides induced by electrostatic interaction with a lipid bilayer membrane

We show that it is possible to induce a defined secondary structure in de novo designed peptides upon electrostatic attachment to negatively charged lipid bilayer vesicles without partitioning of the peptides into the membrane, and that the secondary structure can be varied via small changes in the...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 26(2010), 9 vom: 04. Mai, Seite 6437-48
1. Verfasser: Nygren, Patrik (VerfasserIn)
Weitere Verfasser: Lundqvist, Martin, Liedberg, Bo, Jonsson, Bengt-Harald, Ederth, Thomas
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2010
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Lipid Bilayers Peptides Phosphatidylglycerols 1,2-dioleoyl-sn-glycero-3-phosphoglycerol 66322-31-4 Silicon Dioxide 7631-86-9
Beschreibung
Zusammenfassung:We show that it is possible to induce a defined secondary structure in de novo designed peptides upon electrostatic attachment to negatively charged lipid bilayer vesicles without partitioning of the peptides into the membrane, and that the secondary structure can be varied via small changes in the primary amino acid sequence of the peptides. The peptides have a random-coil conformation in solution, and results from far-UV circular dichroism spectroscopy demonstrate that the structure induced by the interaction with silica nanoparticles is solely alpha-helical and also strongly pH-dependent. The present study shows that negatively charged vesicles, to which the peptides are electrostatically adsorbed via cationic amino acid residues, induce either alpha-helices or beta-sheets and that the conformation is dependent on both lipid composition and variations in peptide primary structure. The pH-dependence of the vesicle-induced peptide secondary structure is weak, which correlates well with small differences in the vesicles' electrophoretic mobility, and thus the surface charge, as the pH is varied
Beschreibung:Date Completed 02.08.2010
Date Revised 18.11.2010
published: Print
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/la100027n