Nanostructured interfacial self-assembly of an amyloid-like peptide

ANYL 176

Patrick Guenoun, Patrick.Guenoun@cea.fr1, Corinne Chevallard2, Mathilde Lepère2, Gerald Brezesinski, Gerald.Brezesinski@mpikg-golm.mpg.de3, Michel Goldmann, michel.goldmann@insp.jussieu.fr4, and Annabel H. Muenter, annabel.muenter@mpikg.mpg.de5. (1) Service de Chimie Moléculaire, LIONS, Bâtiment 125, C.E.A. Saclay F-91191, Gif sur-Yvette Cedex, France, (2) LIONS, DSM/SCM C.E.A. Saclay, C.E.A. Saclay, F-91191 Gif sur Yvette, France, (3) Interface, MPI of Colloids and Interfaces, Am Mühlenberg 1, Potsdam, 14424, (4) INSP Paris, France, (5) Interface Department, Max Planck Institute of Colloids and Interfaces, Research Campus Golm, Potsdam, 14424, Germany
We are interested in making templates which could be used as inducing layers for mineral crystallisation studies inspired by the formation of biominerals. An amyloid-like peptide, named LSFD, was selected and shown to self-assemble with a strong crystalline order when spread as a Langmuir film at the surface of water. This order is related to a ß-sheet conformation of the peptide. When transfered onto a solid substrate, the crystallinity is revealed at a larger scale by Atomic Force Microscopy and, at some pressure surface, LSFD is shown to form a very homogeneous and ordered template like shown in the phase AFM picture included (total width of 500 nm).

 

Directed Assemblies Using Surface Templates
8:25 AM-12:05 PM, Wednesday, April 9, 2008 Morial Convention Center -- Rm. 335, Oral

Division of Analytical Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008