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

Abstract

Feasible and reproducible synthesis of full-length A beta 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 A beta in large quantities at relatively high purity. The amyloidogenic activity of the synthesized A beta was confirmed via thioflavin T assay, transmission electron microscopic analysis and electrophoresis.