bioRxiv· Fang, X., Chalopin, B., Gokturk, S. S., Bhagwani, A. S., Sudareva, M., Molkenbur, R., Tian, W., Feng, M., van Rijt, F. L. H., van Noort, K., Koelewijn, J., Chatziandreou, M., Zhang, B., Merks, J. H. M., Rossig, C., Meissner, R., Janda, C. Y. ·· 16 hours agoPickScore54
Domain-resolved epitope mapping of B7-H3-targeting VHH-Fcs defines isoform-selective binders for antibody-drug conjugate development
In brief
The authors generated six B7-H3-targeting VHH-Fcs. Domain-resolved epitope mapping and deep mutational scanning showed these binders have 10- to 100-fold higher affinity for the 4Ig isoform than the 2Ig isoform, whereas the clinical antibodies ifinatamab, mirzotamab and vobramitamab showed no such selectivity.
Why it matters
Domain-resolved epitope mapping and deep mutational scanning dissect how affinity, epitope and internalization independently contribute to ADC potency.
Source: bioRxiv