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A modified protocol to prepare seed-free starting solutions of amyloid-β (Aβ)₁₋₄₀ and Aβ₁₋₄₂ from the corresponding depsipeptides.

著者 Beeg M , Stravalaci M , Bastone A , Salmona M , Gobbi M
Anal Biochem.2011 Apr 15 ; 411(2):297-9.
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Department of Biochemistry and Molecular Pharmacology, Instituto di Ricerche Farmacologiche "Mario Negri", 20156 Milano, Italy. marten.beeg@chem.ethz.ch

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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.
PMID: 21185802 [PubMed - indexed for MEDLINE]
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