Traceless Purification and Desulfurization of Tau Protein Ligation Products

O. Reimann, C. Smet-Nocca, Christian P. R. Hackenberger – 2015

We present a novel strategy for the traceless purification and synthetic modification of peptides and proteins obtained by native chemical ligation. The strategy involves immobilization of a photocleavable semisynthetic biotin–protein conjugate on streptavidin-coated agarose beads, which eliminates the need for tedious rebuffering steps and allows the rapid removal of excess peptides and additives. On-bead desulfurization is followed by delivery of the final tag-free protein product. The strategy is demonstrated in the isolation of a tag-free Alzheimer's disease related human tau protein from a complex EPL mixture as well as a triphosphorylated peptide derived from the C-terminus of tau.

Titel
Traceless Purification and Desulfurization of Tau Protein Ligation Products
Verfasser
O. Reimann, C. Smet-Nocca, Christian P. R. Hackenberger
Datum
2015
Kennung
10.1002/anie.201408674
Zitierweise
Angew. Chem. Int. Ed., 2015, 54, 306–310
Art
Text
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