Acetylcholinesterase triggers the aggregation of PrP 106-126.

@article{Pera2006AcetylcholinesteraseTT,
  title={Acetylcholinesterase triggers the aggregation of PrP 106-126.},
  author={Marta Pera and Shilina A Roman and M. Ratia and Pelayo Camps and Diego Mu{\~n}oz-Torrero and Laura Colombo and C. Manzoni and Mario Salmona and A. Bernat Bad{\'i}a and M Vict{\`o}ria Clos},
  journal={Biochemical and biophysical research communications},
  year={2006},
  volume={346 1},
  pages={89-94}
}
Acetylcholinesterase (AChE), a senile plaque component, promotes amyloid-beta-protein (Abeta) fibril formation in vitro. The presence of prion protein (PrP) in Alzheimer's disease (AD) senile plaques prompted us to assess if AChE could trigger the PrP peptides aggregation as well. Consequently, the efficacy of AChE on the PrP peptide spanning-residues 106-126 aggregation containing a coumarin fluorescence probe (coumarin-PrP 106-126) was studied. Kinetics of coumarin-PrP 106-126 aggregation… CONTINUE READING