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Amyloid
The Journal of Protein Folding Disorders
Volume 19, 2012 - Issue 3
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Original Article

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

, , , &
Pages 133-137 | Received 30 Sep 2011, Accepted 01 Jun 2012, Published online: 16 Jul 2012
 

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.

Acknowledgements

The authors would like to thank Dr. Jason Moss for his contributions and advice in SPPS route modification.

Declaration of Interest: This work was supported by the Korea Institute of Science and Technology (2V02950 and 2E22310).

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