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Polymerization of tau peptides into fibrillar structures. The effect of FTDP‐17 mutations
Author(s) -
Arrasate Monserrat,
Pérez Mar,
Armas-Portela Rosario,
Ávila Jesús
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00210-0
Subject(s) - peptide , heparin , chemistry , chondroitin sulfate , biophysics , tau protein , mutation , microtubule , biochemistry , gene , microbiology and biotechnology , biology , glycosaminoglycan , alzheimer's disease , medicine , disease
The peptides corresponding to the four repeats found in the microtubule binding region of tau protein were synthesized and their ability for self‐aggregation in presence of heparin or chondroitin sulfate was measured. Mainly, only the peptide containing the third tau repeat is able to form polymers in a high proportion. Additionally, the peptide containing the second repeat aggregates with a very low efficiency. However, when this peptide contains the mutation (P301L), described in a fronto temporal dementia, it is able to form polymers at a higher extent. Finally, it is suggested to have a role for the first and fourth tau repeats. It could be to decrease the ability of the third tau repeat for self‐aggregation in the presence of heparin.