β-amyloids are amphiphilic peptides with a hydrophilic N-terminal domain (residues 1 to 28) and a hydrophobic C-terminal (residues 29 to 40-42), the latter corresponding to a part of the transmembrane domain of APP.1 β-Amyloid assembly into fibrils is initiated by a conformational transition from random coil to β-sheet (hence the name β-amyloid) and a nucleation-dependent aggregation process.1 Aβ peptides that are 39 to 42 amino acid residues in length with a molecular mass of approximately 4 kDa are the core components of neuritic plaques seen in Alzheimer’s disease (AD) brains. Studies have found that dissolving in HFIP favors alpha helical structure and tends to be monomeric.2 HFIP treatment of lyophilized Aβ-peptide results in a dense, homogeneous preparation of unaggregated peptide and samples can be stored as peptide films.3
1. Jarrett, JT. et al. Biochem 32, 4693 (1993).
2. Barrow, CL. et al. J Mol Bio 225, 1075 (1992).
3. Stine, WB. et al. J. Biol. Chem., 278, 11612 (2003).
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