Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations

FEBS Lett. 1999 Mar 5;446(1):199-202. doi: 10.1016/s0014-5793(99)00210-0.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Dimerization
  • Microtubules / chemistry
  • Molecular Sequence Data
  • Mutation
  • Protein Folding
  • tau Proteins / chemistry*
  • tau Proteins / genetics

Substances

  • tau Proteins