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

Ji Won Choi, Hye Yun Kim, Mijin Jeon, Dong Jin Kim, Youngsoo Kim

Research output: Contribution to journalArticle

12 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)133-137
Number of pages5
JournalAmyloid
Volume19
Issue number3
DOIs
Publication statusPublished - 2012 Sep 1

Fingerprint

Solid-Phase Synthesis Techniques
Dimethyl Sulfoxide
Phenylalanine
Amyloid
Electrophoresis
Alzheimer Disease
Electrons
Peptides
Research
thioflavin T

All Science Journal Classification (ASJC) codes

  • Internal Medicine

Cite this

Choi, Ji Won ; Kim, Hye Yun ; Jeon, Mijin ; Kim, Dong Jin ; Kim, Youngsoo. / Efficient access to highly pure β-amyloid peptide by optimized solid-phase synthesis. In: Amyloid. 2012 ; Vol. 19, No. 3. pp. 133-137.
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Efficient access to highly pure β-amyloid peptide by optimized solid-phase synthesis. / Choi, Ji Won; Kim, Hye Yun; Jeon, Mijin; Kim, Dong Jin; Kim, Youngsoo.

In: Amyloid, Vol. 19, No. 3, 01.09.2012, p. 133-137.

Research output: Contribution to journalArticle

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