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Siegmund V.,TU Darmstadt | Schmelz S.,Helmholtz Center for Infection Research | Dickgiesser S.,TU Darmstadt | Beck J.,TU Darmstadt | And 9 more authors.
Angewandte Chemie - International Edition | Year: 2015

Based on the crystal structure of a natural protein substrate for microbial transglutaminase, an enzyme that catalyzes protein crosslinking, a recognition motif for site-specific conjugation was rationally designed. Conformationally locked by an intramolecular disulfide bond, this structural mimic of a native conjugation site ensured efficient conjugation of a reporter cargo to the therapeutic monoclonal antibody cetuximab without erosion of its binding properties. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


PubMed | Merck KGaA, Fachbereich Chemie und Biotechnologie, Helmholtz Center for Infection Research, TU Darmstadt and University of Gottingen
Type: Journal Article | Journal: Angewandte Chemie (International ed. in English) | Year: 2015

Based on the crystal structure of a natural protein substrate for microbial transglutaminase, an enzyme that catalyzes protein crosslinking, a recognition motif for site-specific conjugation was rationally designed. Conformationally locked by an intramolecular disulfide bond, this structural mimic of a native conjugation site ensured efficient conjugation of a reporter cargo to the therapeutic monoclonal antibody cetuximab without erosion of its binding properties.

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