Inhibition of homophilic dimerization and disruption of cell adhesion by P-cadherin-specific small molecules from SPR-based assays

The inhibitor for the homophilic dimerization of P-cadherin was discovered by SPR-based screening using fragment compounds. Our SPR assays identified a specific P-cadherin binder, which was able to inhibit the cell adhesion of living CHO cells that expressed P-cadherin. Our SPR-based screening ident...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2018, Vol.54 (42), p.535-5353
Main Authors: Senoo, Akinobu, Nagatoishi, Satoru, Moberg, Anna, Babol, Linnea Nygren, Mitani, Tomoya, Tashima, Takumi, Kudo, Shota, Tsumoto, Kouhei
Format: Article
Language:English
Subjects:
Animals
Biological Assay
Cadherins - antagonists & inhibitors
Cadherins - immunology
Cell adhesion
Cell adhesion & migration
Cell Adhesion - drug effects
Cell Aggregation - drug effects
CHO Cells
Cricetulus
Dimerization
Immunoassay
Isonicotinic Acids - pharmacology
Molecular chains
Nicotinic Acids - pharmacology
Protein Multimerization
Single-Chain Antibodies - immunology
Surface Plasmon Resonance
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Summary:The inhibitor for the homophilic dimerization of P-cadherin was discovered by SPR-based screening using fragment compounds. Our SPR assays identified a specific P-cadherin binder, which was able to inhibit the cell adhesion of living CHO cells that expressed P-cadherin. Our SPR-based screening identified a compound which was able to inhibit cell adhesion mediated by homophilic dimerization of P-cadherin.
ISSN:1359-7345
1364-548X
DOI:10.1039/c8cc01964a