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

Marten Beeg, Matteo Stravalaci, Antonio Bastone, Mario Salmona, Marco Gobbi

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

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
Volume411
Issue number2
DOIs
Publication statusPublished - Apr 15 2011

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Depsipeptides
Amyloid
Seed
Seeds
Peptides
Circular Dichroism
Dissolution
Agglomeration
Water

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology

Cite this

A modified protocol to prepare seed-free starting solutions of amyloid-β (Aβ) 1-40 and Aβ 1-42 from the corresponding depsipeptides. / Beeg, Marten; Stravalaci, Matteo; Bastone, Antonio; Salmona, Mario; Gobbi, Marco.

In: Analytical Biochemistry, Vol. 411, No. 2, 15.04.2011, p. 297-299.

Research output: Contribution to journalArticle

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