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In situ imaging of quantum dot-AZD4547 conjugates for tracking the dynamic behavior of fibroblast growth factor
Gyoyeon Hwang1,2, Hyeonhye Kim1, Hojong Yoon1
1Chemical Kinomics Research Center, Materials and Life Science Research Division, Korea Institute of Science and Technology, Seoul.
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.
Insights
A novel quantum dot (QD) probe visualizes fibroblast growth factor receptor (FGFR) inhibitor interactions in cells. This tool aids understanding FGFR binding behaviors and developing drug screening strategies.
Area of Science:
- Biochemistry
- Cell Biology
- Nanotechnology
Background:
- Fibroblast growth factor receptors (FGFRs) are crucial for cell functions and are targeted by cancer therapeutics.
- Characterizing the interaction between FGFRs and their inhibitors is vital but challenging.
- Existing methods lack detailed in situ characterization of FGFR-inhibitor interactions.
Purpose of the Study:
- To develop a novel imaging probe for characterizing FGFR-inhibitor interactions.
- To investigate the binding behavior of FGFR3 with the FGFR inhibitor AZD4547.
- To establish a tool for future high-content, cell-based drug screening.
Main Methods:
- Development of a kinase-inhibitor-modified quantum dot (QD) probe.
- Overexpression of turbo-green fluorescent protein-FGFR3 in HeLa cells.
- In situ cellular imaging to assess colocalization of FGFR3 and AZD4547 using the QD probe.
Main Results:
- The QD-AZD4547 probe demonstrated strong, stable signal properties for in situ imaging.
- Successful colocalization of FGFR3 and AZD4547 was observed in HeLa cells.
- The probe effectively visualized the binding behaviors of FGFR3 with the FGFR inhibitor.
Conclusions:
- The inhibitor-modified QD probe is a valuable tool for studying FGFR-inhibitor interactions.
- This approach facilitates a deeper understanding of molecular binding dynamics.
- The probe shows promise for advancing cell-based drug screening strategies for FGFR inhibitors.
