| Autor: |
Marculescu, Cristina, Lakshminarayanan, Abirami, Gault, Joseph, Knight, James C., Folkes, Lisa K., Spink, Thomas, Robinson, Carol V., Vallis, Katherine, Davis, Benjamin G., Cornelissen, Bart |
| Zdroj: |
Chemical Communications; 9/28/2019, Vol. 55 Issue 76, p11342-11345, 4p |
| Abstrakt: |
Site-selective labelling of antibodies (Abs) can circumvent problems from heterogeneity of conventional conjugation. Here, we evaluate the industrially-applied chemoenzymatic 'Q-tag' strategy based on transglutaminase-mediated (TGase) amide-bond formation in the generation of 89Zr-radiolabelled antibody conjugates. We show that, despite previously suggested high regioselectivity of TGases, in the anti-Her2 Ab Herceptin™ more precise native MS indicates only 70–80% functionalization at the target site (Q298H), in competition with modification at other sites, such as Q3H critically close to the CDR1 region. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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