Abstract
Fibroblast growth factor receptors (FGFRs) play an important role in determining cell proliferation, differentiation, migration, and survival. Although a variety of small-molecule FGFR inhibitors have been developed for cancer therapeutics, the interaction between FGFRs and FGFR inhibitors has not been well characterized. The FGFR–inhibitor interaction can be characterized using a new imaging probe that has strong, stable signal properties for in situ cellular imaging of the interaction without quenching. We developed a kinase–inhibitor-modified quantum dot (QD) probe to investigate the interaction between FGFR and potential inhibitors. Especially, turbo-green fluorescent protein-FGFR3s were overexpressed in HeLa cells to investigate the colocalization of FGFR3 and AZD4547 using the QD-AZD4547 probe. The result indicates that this probe is useful for investigating the binding behaviors of FGFR3 with the FGFR inhibitor. Thus, this new inhibitor-modified QD probe is a promising tool for understanding the interaction between FGFR and inhibitors and for creating future high-content, cell-based drug screening strategies.
Original language | English |
---|---|
Pages (from-to) | 5345-5357 |
Number of pages | 13 |
Journal | International Journal of Nanomedicine |
Volume | 12 |
DOIs | |
Publication status | Published - 2017 Jul 26 |
Keywords
- AZD4547
- Fibroblast growth factor 3
- In situ imaging
- Inhibitor
- Kinase
- Quantum dot
ASJC Scopus subject areas
- Biophysics
- Bioengineering
- Biomaterials
- Pharmaceutical Science
- Drug Discovery
- Organic Chemistry