The development of specific agents against amyloidoses requires an understanding of the structure and dynamics of fibrillogenic peptides in different environments on a microscopic level. The 12-residue peptide with the sequence LSFDNSGAITIG-NH2 (“LSFD” peptide), derived from a fragment of the adenovirus tailspike protein, is known to form amyloid-like fibrils in vitro. Whereas x-ray data show the sequence to form a beta-hairpin when embedded in the parent protein, the structure of an isolated LSFD peptide in water is not known. I will present results from simulations of the folding of LSFD in water or a water/vapor interface and the dimerization of LSFD in water.
MPI- Golm