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

• Published in: PloS one Vol. 2; no. 5; p. e479
• Main Authors: Yaghmur, Anan, Laggner, Peter, Zhang, Shuguang, Rappolt, Michael
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 30.05.2007; Public Library of Science (PLoS)
• Subjects: Acids; Alanine; Amino acids; Anions; Aquaporins; Aspartate; Aspartic acid; Biochemistry; Biochemistry/Experimental Biophysical Methods; Biophysics; Biophysics/Experimental Biophysical Methods; Biotechnology; Biotechnology/Small Molecule Chemistry; Cationic peptides; Cations; Chemical Biology/Small Molecule Chemistry; Chemistry; Chemistry/Applied Chemistry; Chemistry/Physical, Inorganic, and Analytical Chemistry; Curvature; E coli; Escherichia coli; Hexagonal phase; Hydration; Hydrocarbons; Hydrophobicity; Lipid Bilayers; Lipids; Lipids - chemistry; Lysine; Membranes; Models, Molecular; Molecular structure; Peptides; Peptides - chemistry; Physics/Condensed Matter; Pollutants; Scattering, Radiation; Small angle X ray scattering; Stability; Studies; Surface active agents; Surface activity; Surface-Active Agents - chemistry; Surfactants; Temperature; X-ray scattering
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0000479

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<or=0.2) and temperatures (25 to 70 degrees C). We demonstrate that the bilayer curvature and the stability are modulated by: i) the peptide/lipid molar ratio, ii) the peptide molecular structure (the degree of hydrophobicity, the type of the hydrophilic amino acid, and the headgroup location), and iii) the temperature. The anionic peptide surfactants, A(6)D and DA(6), exhibit the strongest surface activity. At low peptide concentrations (R = 0.01), the Pn3m structure is still preserved, but its lattice increases due to the strong electrostatic repulsion between the negatively charged peptide molecules, which are incorporated into the interface. This means that the anionic peptides have the effect of enlarging the water channels and thus they serve to enhance the accommodation of positively charged water-soluble active molecules in the Pn3m phase. At higher peptide concentration (R = 0.10), the lipid bilayers are destabilized and the structural transition from the Pn3m to the inverted hexagonal phase (H(2)) is induced. For the cationic peptides, our study illustrates how even minor modifications, such as changing the location of the headgroup (A(6)K vs. KA(6)), affects significantly the peptide's effectiveness. Only KA(6) displays a propensity to promote the formation of H(2), which suggests that KA(6) molecules have a higher degree of incorporation in the interface than those of A(6)K.