Synthesis and Purification of Highly Hydrophobic Peptides Derived from  the C-Terminus of Amyloid β-Protein

Synthesis and Purification of Highly Hydrophobic Peptides Derived from the C-Terminus of Amyloid β-Protein

  • نوع فایل : کتاب
  • زبان : انگلیسی
  • مؤلف : M.M. Condron1, B.H. Monien1 and G. Bitan2,3,*
  • چاپ و سال / کشور: 2008

Description

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 ..-protein (A..42), a peptide believed to be the primary cause for Alzheimer’s disease (AD). The series of C-terminal fragments (CTFs) had the general formula A..(x-42), x=28-39, which potentially can be used as inhibitors of A..42 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.
The Open Biotechnology Journal, 2008, 2, 87-93
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