Locked by Design: A Conformationally Constrained Transglutaminase Tag Enables Efficient Site-Specific Conjugation.

Abstract

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.

DOI: 10.1002/anie.201504851

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@article{Siegmund2015LockedBD, title={Locked by Design: A Conformationally Constrained Transglutaminase Tag Enables Efficient Site-Specific Conjugation.}, author={Vanessa Siegmund and Stefan Schmelz and Stephan Dickgiesser and Jan Beck and Aileen Ebenig and Heiko Fittler and Holm Frauendorf and Birgit Piater and Ulrich A. K. Betz and Olga Avrutina and Andrea Scrima and H L Fuchsbauer and Harald Kolmar}, journal={Angewandte Chemie}, year={2015}, volume={54 45}, pages={13420-4} }