Molecular Characterization of the Recombinant Ig1 Axl Receptor Domain: An Intriguing Bait for Screening in Drug
Rossella Di Stasi1, Lucia De Rosa1, Guido Izzi1
1Istituto di Biostrutture e Bioimmagini, CNR-Consiglio Nazionale delle Ricerche, Via Pietro Castellino 111, 80131 Napoli, Italy.
Abstract:
Axl receptor tyrosine kinase and its ligand Gas6 regulate several biological processes and are involved in both the onset and progression of tumor malignancies and autoimmune diseases. Based on its key role in these settings, Axl is considered a promising target for the development of molecules with therapeutic and diagnostic purposes. In this paper, we describe the molecular characterization of the recombinant Ig1 domain of Axl (Ig1 Axl) and its biochemical properties. For the first time, an exhaustive spectroscopic characterization of the recombinant protein through circular dichroism and fluorescence studies is also reported, as well as a binding analysis to its natural ligand Gas6, paving the way for the use of recombinant Ig1 Axl as a bait in drug discovery screening procedures aimed at the identification of novel and specific binders targeting the Axl receptor.
Insights
Researchers characterized the Ig1 domain of Axl receptor tyrosine kinase (Axl), a key target in cancer and autoimmune diseases. This work enables new drug discovery screening for Axl-targeting therapeutics.
Area of Science:
- Biochemistry
- Molecular Biology
- Drug Discovery
Background:
- Axl receptor tyrosine kinase (Axl) and its ligand Gas6 are implicated in tumor progression and autoimmune diseases.
- Axl is a promising therapeutic and diagnostic target due to its role in disease pathogenesis.
- Understanding Axl's molecular interactions is crucial for developing targeted therapies.
Purpose of the Study:
- To perform molecular characterization of the recombinant Ig1 domain of Axl (Ig1 Axl).
- To investigate the biochemical and spectroscopic properties of Ig1 Axl.
- To analyze the binding affinity of Ig1 Axl to its natural ligand Gas6.
Main Methods:
- Recombinant protein expression and purification of Ig1 Axl.
- Spectroscopic characterization using circular dichroism (CD) and fluorescence spectroscopy.
- Biochemical assays to assess binding to Gas6.
Main Results:
- Successful molecular and biochemical characterization of recombinant Ig1 Axl.
- Detailed spectroscopic analysis providing insights into protein structure and stability.
- Demonstrated binding of Ig1 Axl to its ligand Gas6.
Conclusions:
- The characterized recombinant Ig1 Axl is suitable for use as a bait in drug discovery.
- This study lays the foundation for identifying novel, specific binders targeting the Axl receptor.
- The findings facilitate the development of new therapeutic and diagnostic agents targeting Axl.
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