Structural Bioinformatics and Molecular Modeling
CRBM-CNRS Montpellier


Several lines of evidence suggest that amyloid fibrils play a causative role in several neurodegenerative diseases, including Alzheimer, Parkinson and Hungtington deseases. Despite a number of efforts, an understanding of the structure and mechanism of amyloid fibril formation remains elusive. This dilemma may be attributed to the fact that methods of high resolution structure determination - X-ray crystallography and NMR spectroscopy - cannot be used on account of the polymeric character and insolubility of the fibrils. The determination of the fibril structure goes throughout suggestions of structural models in the process of accumulation of experimental evidences, until a unique model can explain the whole set of data.

We are contributing to the progress in this field by developing structural models for the amyloid and prion fibrils. Our ultimate goals are a structure based prediction of amyloidogenic properties of amino acid sequences and rational design of the fibrillogenesis inhibitors.