Aβ Produced as a Fusion to Maltose Binding Protein Can Be Readily Purified and Stably Associates with Copper and Zinc

Author(s): J. Caine, I. Volitakis, R. Cherny, J. Varghese, I. Macreadie.

Journal Name: Protein & Peptide Letters

Volume 14 , Issue 1 , 2007

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Abstract:

The 42 amino acid Alzheimers Aβ peptide has been produced in E. coli as a soluble fusion to maltose binding protein (MBP). Affinity purification on amylose columns of MBP-Aβ and MBP led to the recovery of proteins at purities that were suited for physicochemical analyses. MBP-Aβ was able to bind approximately 2 mole equivalents of copper or 4 mole equivalents of zinc, while MBP alone bound negligible amounts of zinc or copper. We conclude that A can bind 2 copper or 4 zinc ions in its fusion format. Because MBP-Aβ is a convenient protein to work with, this system is well suited for further studies on the structure of Aβ and its interactions with metals.

Keywords: Alzheimer's disease, amyloid peptide, copper binding, zinc binding

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Article Details

VOLUME: 14
ISSUE: 1
Year: 2007
Page: [83 - 86]
Pages: 4
DOI: 10.2174/092986607779117263

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