Dresden 2003 – wissenschaftliches Programm
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SYCN: Computational nanoscience - from materials to biology
SYCN 102: Computational Nanoscience: From Materials to Biology (Poster, gemeinsam mit SYSE)
SYCN 102.23: Poster
Dienstag, 25. März 2003, 19:00–21:00, ZEU/160
β-helices as putative structural motifs in neurodegenerative diseases involving amyloid plaques: Structural stability studied by MD-simulations — •Martina Stork and Paul Tavan — Chair for BioMolecular Optics, University of Munich, Oettingenstr. 67, D-80538 Muenchen
The mechanisms of amyloid formation in neurodegenerative diseases like BSE or morbus Huntington are unclear, as the structure of the insoluble amyloid fibres so far are inaccessible to highly resolved structure determination. Recently, both electron diffraction of two-dimensional PrPSc-crystals [1] and a new interpretation of x-ray data of poly-L-glutamine [2] pointed to a common structural motif of amyloid fibres, called β-helices.
By MD-simulations we have investigated wether there exists a preferred number of amino acids per helical turn and a preferred geometry for β-helical structures. We have modelled small peptides of poly-L-glutamine by different two-layered β-helical structures and have carried out extended MD-simulations. To clarify wether short β-helical peptides are structurally stable, we have simulated fragments of a known stable β-helical structure and have compared their structural stability to our amyloid models.
[1] H. Wille et al., Proc. Natl. Acad. Sci. USA 99(6): 3563-3568 (2002)
[2] M.F. Perutz et al., Proc. Natl. Acad. Sci. USA 99(8): 5591-5595 (2002)