Berlin 2005 – wissenschaftliches Programm
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AKB: Biologische Physik
AKB 100: Poster Session I
AKB 100.7: Poster
Samstag, 5. März 2005, 16:45–18:45, Poster TU D
Self-assembled peptide fibrils as novel biomaterials — •Patrick Mesquida1, Rachel McKendry1, and Cait MacPhee2 — 1Department of Medicine, University College London, UK — 2Department of Physics, University of Cambridge, UK
Amyloid fibrils are self-assembled, beta-sheet-rich superstructures of peptides or proteins. Although these aggregates have first been found in connection with protein-misfolding diseases there is evidence that the ability to form fibrils is a thermodynamic property of any polypeptide chain rather than a result of specific, disease-related amino-acid sequences. Fibrils can easily be formed in-vitro from non-disease-related proteins and even from artificially "bottom-up"-synthesized peptide chains which have no biological function at all. Furthermore, functional groups can be incorporated without significantly disturbing the fibril superstructure. This is why amyloid fibrils have recently attracted considerable interest as potentially useful, novel biomaterial. Here, we present investigations of the physical properties of a specific fibrillar system, which forms well-defined nanorods of ca 10nm diameter, and of its interaction with surfaces.