Quantitative determination of the topological propensities of amyloidogenic peptides.

@article{Shi2006QuantitativeDO,
  title={Quantitative determination of the topological propensities of amyloidogenic peptides.},
  author={Yuan Shi and Pieter F. W. Stouten and Nirmala Pillalamarri and Lauren Barile and Ramon V. Rosal and Saul Teichberg and Zimei Bu and David J. E. Callaway},
  journal={Biophysical chemistry},
  year={2006},
  volume={120 1},
  pages={55-61}
}
One of the interesting puzzles of amyloid beta-peptide of Alzheimer's disease (Abeta) is that it appears to polymerize into amyloid fibrils in a parallel beta sheet topology, while smaller subsets of the peptide produce anti-parallel beta sheets. In order to target potential weak points of amyloid fibrils in a rational drug design effort, it would be helpful to understand the forces that drive this change. We have designed two peptides CHQKLVFFAEDYNGKDEAFFVLKQHW and CHQKLVFFAEDYNGKHQKLVFFAEDW… CONTINUE READING