X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin

@inproceedings{Kreutzer2016XrayCS,
  title={X-ray
Crystallographic Structures of a Trimer,
Dodecamer, and Annular Pore Formed by an Aβ17–36 β-Hairpin},
  author={Adam G Kreutzer and Imane L. Hamza and Ryan K Spencer and James S Nowick},
  booktitle={Journal of the American Chemical Society},
  year={2016}
}
High-resolution structures of oligomers formed by the β-amyloid peptide Aβ are needed to understand the molecular basis of Alzheimer's disease and develop therapies. This paper presents the X-ray crystallographic structures of oligomers formed by a 20-residue peptide segment derived from Aβ. The development of a peptide in which Aβ17-36 is stabilized as a β-hairpin is described, and the X-ray crystallographic structures of oligomers it forms are reported. Two covalent constraints act in tandem… CONTINUE READING

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Analytical HPLC trace of peptide 2. S17 Mass spectra of peptide 2. S18 S19 Characterization of peptide 3

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Analytical HPLC trace of peptide 3. S20 Mass spectra of peptide 3. S21 S22 Characterization of peptide 4

  • Analytical HPLC trace of peptide 3. S20 Mass…

Analytical HPLC trace of peptide 4. S23 Mass spectra of peptide 4

  • Analytical HPLC trace of peptide 4. S23 Mass…

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