Preparing synthetic Aβ in different aggregation states.

@article{Stine2011PreparingSA,
  title={Preparing synthetic Aβ in different aggregation states.},
  author={William Blaine Stine and Lisa M. Jungbauer and Chunjiang Yu and Mary Jo Ladu},
  journal={Methods in molecular biology},
  year={2011},
  volume={670},
  pages={
          13-32
        }
}
This chapter outlines protocols that produce homogenous preparations of oligomeric and fibrillar amyloid-β peptide (Aβ). While there are several isoforms of this peptide, the 42 amino acid form is the focus because of its genetic and pathological link to Alzheimer's disease (AD). Past decades of AD research highlight the dependence of Aβ42 function on its structural assembly state. Biochemical, cellular and in vivo studies of Aβ42 usually begin with purified peptide obtained by chemical… CONTINUE READING
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