Influence of aggregation propensity and stability on amyloid fibril formation as studied by Fourier transform infrared spectroscopy and two-dimensional COS analysis.

@article{CerdCosta2009InfluenceOA,
  title={Influence of aggregation propensity and stability on amyloid fibril formation as studied by Fourier transform infrared spectroscopy and two-dimensional COS analysis.},
  author={N{\'u}ria Cerd{\`a}-Costa and Igor de la Arada and Francesc X. Avil{\'e}s and Jos{\'e} Luis R. Arrondo and Sandra Villegas},
  journal={Biochemistry},
  year={2009},
  volume={48 44},
  pages={10582-90}
}
Understanding the process of amyloidogenesis is important for the future treatment of misfolding-based diseases, such as Alzheimer's, spongiform encephalopathies, and other important disorders affecting humans. In this work, we have used one of the best-characterized models for folding and misfolding, the activation domain of human procarboxypeptidase A2 (ADA2h). The wild type (WT) and three mutants affecting the kinetics of aggregation have been studied by IR from the folded state at acidic pD… CONTINUE READING