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.
Stine, W.B. et al. J. Biol. Chem., 278, 11612 (2003).
Sequence (One-Letter Code)
Sequence (Three-Letter Code)
H - Asp - Ala - Glu - Phe - Arg - His - Asp - Ser - Gly - Tyr - Glu - Val - His - His - Gln - Lys - Leu - Val - Phe - Phe - Ala - Glu - Asp - Val - Gly - Ser - Asn - Lys - Gly - Ala - Ile - Ile - Gly - Leu - Met - Val - Gly - Gly - Val - Val - Ile - Ala-OH