The efficient synthesis and purification of amyloid-β(1-42) using an oligoethylene glycol-containing photocleavable lysine tag

John A Karas; Asif Noor; Christine Schieber; Timothy U Connell; Frances Separovic; Paul S Donnelly

doi:10.1039/c7cc03147e

The efficient synthesis and purification of amyloid-β(1-42) using an oligoethylene glycol-containing photocleavable lysine tag

Chem Commun (Camb). 2017 Jun 22;53(51):6903-6905. doi: 10.1039/c7cc03147e.

Authors

John A Karas¹, Asif Noor², Christine Schieber², Timothy U Connell², Frances Separovic², Paul S Donnelly²

Affiliations

¹ School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, VIC 3010, Australia. jkaras@unimelb.edu.au pauld@unimelb.edu.au and Department of Chemical and Biomolecular Engineering, The University of Melbourne, VIC 3010, Australia.
² School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, VIC 3010, Australia. jkaras@unimelb.edu.au pauld@unimelb.edu.au.

PMID: 28607975
DOI: 10.1039/c7cc03147e

Abstract

A short, monodisperse oligoethylene glycol-containing photocleavable lysine tag was developed to facilitate the efficient purification of hydrophobic and fibril-forming peptides. This new tag was used to prepare a modified Aβ₄₂ peptide with increased solubility and decreased propensity to aggregate in aqueous media. The solubilising tag was readily removed by irradiation with UV light and permitted the preparation and isolation of Aβ₄₂ in high purity and yield.