Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants.
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ABSTRACT:
SUBMITTER: Yaghmur A
PROVIDER: S-EPMC1868779 | biostudies-other | 2007
REPOSITORIES: biostudies-other
Publications
Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants.
Yaghmur Anan A Laggner Peter P Zhang Shuguang S Rappolt Michael M
PloS one 20070530 5
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 ternar ...[more]
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