Controlling aggregation propensity in A53T mutant of alpha-synuclein causing Parkinson's disease.

@article{Kumar2009ControllingAP,
  title={Controlling aggregation propensity in A53T mutant of alpha-synuclein causing Parkinson's disease.},
  author={Sonu Kumar and Anita Sarkar and Durai Sundar},
  journal={Biochemical and biophysical research communications},
  year={2009},
  volume={387 2},
  pages={305-9}
}
Understanding alpha-synuclein in terms of fibrillization, aggregation, solubility and stability is fundamental in Parkinson's disease (PD). The three familial mutations, namely, A30P, E46K and A53T cause PD because the hydrophobic regions in alpha-synuclein acquire beta-sheet configuration, and have a propensity to fibrillize and form amyloids that cause cytotoxicity and neurodegeneration. On simulating the native form and mutants (A30P, E46K and A53T) of alpha-synuclein in water solvent, clear… CONTINUE READING