Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants

TY - JOUR

T1 - Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants

AU - Yaghmur, Anan

AU - Laggner, Peter

AU - Zhang, Shuguang

AU - Rappolt, Michael

PY - 2007

Y1 - 2007

N2 - This study reports the effect of loading four different charged designer lipid-like short anionic and cationic peptide surfactants on the fully hydrated monoolein (MO)-based Pn3m phase (Q(224)). The studied peptide surfactants comprise seven amino acid residues, namely A(6)D, DA(6), A(6)K, and KA(6). D (aspartic acid) bears two negative charges, K (lysine) bears one positive charge, and A (alanine) constitutes the hydrophobic tail. To elucidate the impact of these peptide surfactants, the ternary MO/peptide/water system has been investigated using small-angle X-ray scattering (SAXS), within a certain range of peptide concentrations (R

AB - This study reports the effect of loading four different charged designer lipid-like short anionic and cationic peptide surfactants on the fully hydrated monoolein (MO)-based Pn3m phase (Q(224)). The studied peptide surfactants comprise seven amino acid residues, namely A(6)D, DA(6), A(6)K, and KA(6). D (aspartic acid) bears two negative charges, K (lysine) bears one positive charge, and A (alanine) constitutes the hydrophobic tail. To elucidate the impact of these peptide surfactants, the ternary MO/peptide/water system has been investigated using small-angle X-ray scattering (SAXS), within a certain range of peptide concentrations (R

KW - Anions

KW - Lipid Bilayers

KW - Lipids

KW - Models, Molecular

KW - Peptides

KW - Scattering, Radiation

KW - Surface-Active Agents

KW - Temperature

U2 - 10.1371/journal.pone.0000479

DO - 10.1371/journal.pone.0000479

M3 - Journal article

C2 - 17534429

SN - 1932-6203

VL - 2

SP - e479

JO - PLoS Computational Biology

JF - PLoS Computational Biology

IS - 5

ER -