Journal article

A beta produced as a fusion to maltose binding protein can be readily purified and stably associates with copper and zinc

J Caine, I Volitakis, R Cherny, J Varghese, I Macreadie

PROTEIN AND PEPTIDE LETTERS | BENTHAM SCIENCE PUBL LTD | Published : 2007

Abstract

The 42 amino acid Alzheimer's Abeta peptide has been produced in E. coli as a soluble fusion to maltose binding protein (MBP). Affinity purification on amylose columns of MBP-Abeta and MBP led to the recovery of proteins at purities that were suited for physicochemical analyses. MBP-Abeta 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 Abeta can bind 2 copper or 4 zinc ions in its fusion format. Because MBP-Abeta is a convenient protein to work with, this system is well suited for further studies on the structure of Abeta and its interactions with metals.

University of Melbourne Researchers