TAU GLYCATION IS INVOLVED IN AGGREGATION OF THE PROTEIN BUT NOT IN THE FORMATION OF FILAMENTS

A tau peptide, peptide 2R, with capacity for self assembly into filame nts was used as a model to test the role of glycation on tau assembly or aggregation. Our results indicate that glycation of that peptide fa cilitates dimer formation but not assembly into filaments. However, gl ycation of tau results in the bundling of the tau filaments formed by glycosaminoglycan-induced polymerisation. These results suggest a role of glycation in the formation of covalent links among pre-formed fila ments but not in the assembly of those filaments.