Efficient access to highly pure β-amyloid peptide by optimized solid-phase synthesis

Abstract

Feasible and reproducible synthesis of full-length Aβ peptides has been one of the major challenges in Alzheimer's disease research. By using dimethyl sulfoxide as an anti-aggregation solvent and as an agent to promote double-coupling of two phenylalanine that frequently experience residual deletion, we developed a reliable manual Fmoc solid phase peptide synthesis procedure to produce biologically active Aβ in large quantities at relatively high purity. The amyloidogenic activity of the synthesized Aβ was confirmed via thioflavin T assay, transmission electron microscopic analysis and electrophoresis.