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

ABSTRACT: 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

SUBMITTER: Yaghmur A

PROVIDER: S-EPMC1868779 | biostudies-other | 2007

REPOSITORIES: biostudies-other

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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]

PMID: 17534429

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