Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement.

@article{Morimoto2004AnalysisOT,
  title={Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement.},
  author={Akira Morimoto and Kazuhiro Irie and Kazuma Murakami and Yuichi Masuda and Hajime Ohigashi and Masaya Nagao and Hiroyuki Fukuda and Takahiko Shimizu and Takuji Shirasawa},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 50},
  pages={
          52781-8
        }
}
Amyloid fibrils in Alzheimer's disease mainly consist of 40- and 42-mer beta-amyloid peptides (Abeta40 and Abeta42) that exhibit aggregative ability and neurotoxicity. Although the aggregates of Abeta peptides are rich in intermolecular beta-sheet, the precise secondary structure of Abeta in the aggregates remains unclear. To identify the amino acid residues involved in the beta-sheet formation, 34 proline-substituted mutants of Abeta42 were synthesized and their aggregative ability and… CONTINUE READING

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