Tuning curvature and stability of monoolein bilayers by designer lipid-like peptide surfactants |
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Authors: | Yaghmur Anan Laggner Peter Zhang Shuguang Rappolt Michael |
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Institution: | Institute of Biophysics and Nanosystems Research (IBN), Austrian Academy of Sciences, Graz, Austria. anan.yaghmur@oeaw.ac.at |
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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
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