Removal of any preexisting structures in lyophilized stocks of Aβ-peptide is the critical initial step for controlled aggregation studies. HFIP has been shown to break down β-sheet structure, disrupt hydrophobic forces in aggregated amyloid preparations, and promotes α-helical secondary structure. HFIP treatment of lyophilized Aβ-peptide resulted in a dense, homogeneous preparation of unaggregated peptide and samples can be stored as peptide films.
Proteins & Peptides
Peak Area by HPLC ≥95%
Ref: Stine, W.B. et al. J. Biol. Chem., 278, 11612 (2003).