Skip to main content

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

Buy Article:

$63.00 plus tax (Refund Policy)


The 42 amino acid Alzheimer's 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

Document Type: Research Article


Affiliations: CSIRO Molecular and Health Technologies, Parkville, Australia.

Publication date: January 1, 2007

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Partial Open Access Content
Partial Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more