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

Akinobu Senoo; Satoru Nagatoishi; Anna Moberg; Linnea Nygren Babol; Tomoya Mitani; Takumi Tashima; Shota Kudo; Kouhei Tsumoto

doi:10.1039/c8cc01964a

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

Chem Commun (Camb). 2018 May 22;54(42):5350-5353. doi: 10.1039/c8cc01964a.

Authors

Akinobu Senoo¹, Satoru Nagatoishi, Anna Moberg, Linnea Nygren Babol, Tomoya Mitani, Takumi Tashima, Shota Kudo, Kouhei Tsumoto

Affiliation

¹ Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

PMID: 29741543
DOI: 10.1039/c8cc01964a

Abstract

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.

MeSH terms

Animals
Biological Assay
CHO Cells
Cadherins / antagonists & inhibitors*
Cadherins / immunology
Cell Adhesion / drug effects*
Cell Aggregation / drug effects
Cricetulus
Dimerization
Immunoassay
Isonicotinic Acids / pharmacology*
Nicotinic Acids / pharmacology*
Protein Multimerization
Single-Chain Antibodies / immunology
Surface Plasmon Resonance

Substances

Cadherins
Isonicotinic Acids
Nicotinic Acids
Single-Chain Antibodies