期刊
ANALYTICAL BIOCHEMISTRY
卷 411, 期 2, 页码 297-299出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2010.12.032
关键词
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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.
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