A modified protocol to prepare seed-free starting solutions of amyloid-β (Aβ) 1-40 and Aβ 1-42 from the corresponding depsipeptides

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Preparing reliable, seed-free stock solutions of the highly amyloidogenic peptides amyloid-β (Aβ) is difficult. Besides the formation of aggregates during synthesis and storage, dissolution of the peptide is a critical step because vortexing can induce aggregation. To overcome this, synthesis of the more water-soluble depsi-Aβ 1-42 peptide, from which the native sequence is easily obtained, has been suggested. We further refined this technique, including a cutoff filtration step and switching the depsipeptide in basic conditions, to stabilize the formed native peptide. The obtained solutions of native Aβ 1-40 and Aβ 1-42 peptides were homogeneous and aggregate free, as indicated by thioflavin T and circular dichroism analysis.

Original languageEnglish
Pages (from-to)297-299
Number of pages3
JournalAnalytical Biochemistry
Issue number2
Publication statusPublished - Apr 15 2011

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology


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