| Autor: |
Grevtsev AS; JSC 'BIOCAD', 198515 St. Peterburg, Russia., Azarian AD; JSC 'BIOCAD', 198515 St. Peterburg, Russia., Misorin AK; JSC 'BIOCAD', 198515 St. Peterburg, Russia., Chernyshova DO; JSC 'BIOCAD', 198515 St. Peterburg, Russia., Iakovlev PA; JSC 'BIOCAD', 198515 St. Peterburg, Russia., Karbyshev MS; JSC 'BIOCAD', 198515 St. Peterburg, Russia. |
| Jazyk: |
angličtina |
| Zdroj: |
Biosensors [Biosensors (Basel)] 2023 Dec 09; Vol. 13 (12). Date of Electronic Publication: 2023 Dec 09. |
| DOI: |
10.3390/bios13121022 |
| Abstrakt: |
The engineering of bispecific antibodies that exhibit optimal affinity and functional activity presents a significant scientific challenge. To tackle this, investigators employ an assortment of protein assay techniques, such as label-free interaction methodologies, which offer rapidity and convenience for the evaluation of extensive sample sets. These assays yield intricate data pertaining to the affinity towards target antigens and Fc-receptors, instrumental in predicting cellular test outcomes. Nevertheless, the fine-tuning of affinity is of paramount importance to mitigate potential adverse effects while maintaining efficient obstruction of ligand-receptor interactions. In this research, biolayer interferometry (BLI) was utilized to probe the functional characteristics of bispecific antibodies targeting cluster of differentiation 47 (CD47) and programmed death-ligand 1 (PD-L1) antigens, encompassing affinity, concurrent binding to two disparate antigens, and the inhibition of ligand-receptor interactions. The findings derived from BLI were juxtaposed with data from in vitro signal regulatory protein-α (SIRP-α)/CD47 blockade reporter bioassays for two leading bispecific antibody candidates, each demonstrating distinct affinity to CD47. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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