• Medicine
  • Published in Biochemistry 2002

Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy.

@article{Nichols2002GrowthOB,
  title={Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy.},
  author={Michael R Nichols and Melissa A. Moss and Dana Kim Reed and Wen-lang Lin and Rajendrani Mukhopadhyay and Jan H. Hoh and Terrone L. Rosenberry},
  journal={Biochemistry},
  year={2002},
  volume={41 19},
  pages={
          6115-27
        }
}
Amyloid plaques in brain tissue are a hallmark of Alzheimer's disease. Primary components of these plaques are 40- and 42-residue peptides, denoted A beta(1-40) and A beta(1-42), that are derived by proteolysis of cellular amyloid precursor protein. Synthetic A beta(1-40) and A beta(1-42) form amyloid fibrils in vitro that share many features with the amyloid in plaques. Soluble intermediates in A beta fibrillogenesis, termed protofibrils, have been identified previously, and here we describe… CONTINUE READING

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