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
Protein & Peptide Letters
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.
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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 |
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