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Publications 2013 - 2015

Orthogonal dual-modification of proteins for the engineering of multivalent protein scaffolds
Citation key 127.2015.muehlberg
Author Mühlberg, M. and Hoesl, M. G. and Kuehne, C. and Dernedde, J. and Budisa, N. and Hackenberger, C. P. R.
Pages 784–791
Year 2015
DOI 10.3762/bjoc.11.88
Journal Beilstein J. Org. Chem
Volume 11
Abstract To add new tools to the repertoire of protein-based multivalent scaffold design, we have developed a novel dual-labeling strategy for proteins that combines residue-specific incorporation of unnatural amino acids with chemical oxidative aldehyde formation at the N-terminus of a protein. Our approach relies on the selective introduction of two different functional moieties in a protein by mutually orthogonal copper-catalyzed azide–alkyne cycloaddition (CuAAC) and oxime ligation. This method was applied to the conjugation of biotin and β-linked galactose residues to yield an enzymatically active thermophilic lipase, which revealed specific binding to Erythrina cristagalli lectin by SPR binding studies.
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