Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.

@article{Liu2004Residues1A,
  title={Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.},
  author={Ruitian Liu and Chad J McAllister and Yuri L Lyubchenko and Michael Sierks},
  journal={Journal of neuroscience research},
  year={2004},
  volume={75 2},
  pages={162-71}
}
We examined the effects of co-incubating nine different Abeta peptide fragments with full-length Abeta1-40 (Abeta40) on protein aggregation. Six fragments enhanced aggregation of Abeta40 (Abeta1-28, 12-28, 17-28, 10-20, 25-35 and 17-40), while three others did not (Abeta1-11, 1-16, and 20-29). All of the peptides that enhanced aggregation contained either residues 17-20 or 30-35, indicating the importance of these regions for promoting aggregation of full-length Abeta. Abeta25-35 in particular… CONTINUE READING

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