Null

Alzheimers treatment by preventing dimerization using protein inhibitors Alzheimers disease is caused by the accumulation of amyloids, or protein fibrils caused by the aggregation of beta-sheets that accumulate as plaques. A strategy for inhibiting aggregation of amyloid beta fibrils is using peptide-baed inhibitors focused on the internal sequence (16-22) KLVFFAE, identified to be responsible for self-association and aggregation. Previous inhibitors used strained proline, N-methylated amino acids, soluble peptides, D-amino acids, and added targeting sequences. A designed OR2 peptide was found to be a good inhibitor, but it required additional modifications to be a viable therapy: Arg at N and C to prevent aggregation of OR2 itself, and making it a "retro-inverso" version with opposite C->N directionality and some amino acids replaced with the D-isomer. http://pubs.acs.org/doi/pdf/10.1021/bi100144m

Currently, we are looking into previous research that's studying:

- other forms of treatment/prevention of aggregation of amyloids (ie. inhibition? active breaking up of aggregates? etc)

- other forms of inhibition for Alzheimers treatment (ie. protein, chemical inhibitors)

- protein inhibitors for other amyloid-based diseases