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

被引：44

作者：

Beeg, Marten ^{[1
]}

Stravalaci, Matteo ^{[1
]}

Bastone, Antonio ^{[1
]}

Salmona, Mario ^{[1
]}

Gobbi, Marco ^{[1
]}

机构：

[1] Ist Ric Farmacol Mario Negri, Dept Mol Pharmacol & Biochem, I-20156 Milan, Italy

来源：

ANALYTICAL BIOCHEMISTRY | 2011年 / 411卷 / 02期

关键词：

ACYL ISOPEPTIDE METHOD; SEQUENCE-CONTAINING PEPTIDES; ALZHEIMERS-DISEASE; ISODIPEPTIDE UNIT; IN-VITRO; PROTEIN; AGGREGATION; FIBRILLOGENESIS; A-BETA-1-42;

D O I：

10.1016/j.ab.2010.12.032

中图分类号：

Q5 [生物化学];

学科分类号：

070307 [化学生物学];

摘要：

Preparing reliable, seed-free stock solutions of the highly amyloidogenic peptides amyloid-beta (A beta) 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-A beta(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 A beta(1-40) and A beta(1-42) Peptides were homogeneous and aggregate free, as indicated by thioflavin T and circular dichroism analysis. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：297 / 299

页数：3

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