PMID: 11308873Apr 20, 2001Paper

Dramatic rigidification of a peptide-decorated lamellar phase

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
N TsapisR Ober

Abstract

We have performed small-angle x-ray scattering on a lamellar (L(alpha)) phase made of a nonionic surfactant (C12E4), decane, and water, after the insertion of a triblock peptide. The hydrophilic part of the peptide is rigid and organized in an alpha helix in the presence of membranes. Surface tension measurements and spectrofluorometry show that the peptide lies on the membrane surface. The Caillé parameter eta and the smectic compressibility modulus (-)B decrease with peptide concentration, whereas the membrane bending rigidity kappa increases threefold for mole ratio of peptide to surfactant as low as 5.2 x 10(-4). The published models for rigid inclusions in membranes cannot account for this dramatic rigidification. However, experimental results are well fitted by a Heuristic renormalization of the membrane thickness.

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Citations

Oct 19, 2005·The European Physical Journal. E, Soft Matter·F Castro-RomanC Ligoure
Apr 27, 2012·Chemistry and Physics of Lipids·Christiane DeckerSylvio May
Jul 25, 2017·The Journal of Chemical Physics·Y KawabataH Seto

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