Author:
Condron M.M.,Monien B.H.,Bitan G.
Abstract
Some biotechnological inventions involve expensive, sophisticated machines. Others are relatively simple innovations
that nevertheless address, and solve difficult problems. Synthesis and purification of highly hydrophobic peptides
can be a difficult and challenging task, particularly when these peptides have low solubility in both aqueous and organic
solvents. Here we describe the synthesis and purification of a series of peptides derived from the hydrophobic Cterminus
of the 42-residue form of amyloid β-protein (Aβ42), a peptide believed to be the primary cause for Alzheimer’s
disease (AD). The series of C-terminal fragments (CTFs) had the general formula Aβ(x-42), x=28-39, which potentially
can be used as inhibitors of Aβ42 assembly and neurotoxicity. Synthesis and purification of peptides containing 8-residues
or less were straightforward. However, HPLC purification of longer peptides was problematic and provided <1% yield in
particularly difficult cases due to very poor solubility in the solvent systems used both in reverse- and in normal phase
chromatography. Modification of the purification protocol using water precipitation followed by removal of scavengers by
washing with diethyl ether circumvented the need for HPLC purification and provided these peptides with purity as high
as HPLC-purified peptides and substantially increased yield.
Publisher
Bentham Science Publishers Ltd.
Subject
Biomedical Engineering,Biochemistry,Bioengineering,Biophysics,Biotechnology
Cited by
23 articles.
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