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

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

Volume: 14 Issue: 1

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

Affiliation:

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

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.

Cite this article as:

Caine J., Volitakis I., Cherny R., Varghese J. and Macreadie I., Aβ Produced as a Fusion to Maltose Binding Protein Can Be Readily Purified and Stably Associates with Copper and Zinc, Protein & Peptide Letters 2007; 14 (1) . https://dx.doi.org/10.2174/092986607779117263

DOI https://dx.doi.org/10.2174/092986607779117263	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305