Regensburg 2007 – wissenschaftliches Programm
Bereiche | Tage | Auswahl | Suche | Downloads | Hilfe
CPP: Fachverband Chemische Physik und Polymerphysik
CPP 20: POSTER: Biological Systems + New Materials
CPP 20.2: Poster
Mittwoch, 28. März 2007, 16:00–18:30, Poster B
Kinetics, intermediates, and mechanisms of the aggregation of amyloid protein systems — •Gudrun Lotze1, Andreas Bögehold2, Bernd Abel2, and Hauke Schollmeyer1 — 1Georg-August Universität Göttingen, Institut für Röntgenphysik, Friedrich-Hund-Platz 1, 37077 Göttingen — 2Georg-August Universität Göttingen, Institut für Physikalische Chemie, Tammannstraße 6, 37077 Göttingen
Neurodegenerative diseases such as Alzheimer's, Parkinson's and the transmissible spongiform encephalopathyies are characterized by abnormal protein aggregates, often in form of highly symmetric amyloid fibrils. Amyloid fibrils are polypeptide aggregates in which the polypeptide backbone is arranged in a specific cross-β sheet quarternary structure. However, the molecular mechanisms and timescales of the formation of intermediates and fibrils are still not fully understood and currently subject of intense research.
Insulin is a well suited model system to analyze the kinetics of fibril formation. We use x-ray scattering and transmission x-ray microscopy to investigate different states (intermediates and fully grown fibrils) of molecular structure and topology of the model system insulin.