Beilstein J. Org. Chem.2015,11, 784–791, doi:10.3762/bjoc.11.88
(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.
Keywords: chemoselectivity; dualprotein
modification; lectin; multivalency; Introduction
The chemical modification of proteins has been developed to a core discipline in chemical biology with diverse applications in all areas of the life sciences, including pharmacology, biophysics, biotechnology and cell biology [1][2][3][4]. In addition to the
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Graphical Abstract
Scheme 1:
Protein design and dual-functionalization of TTL: periodate cleavage, oxime ligation and CuAAC.