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Identification of a RON tyrosine kinase receptor binding peptide using phage display technique and computational
Omid Zarei1,2,3, Silvia Benvenuti4, Fulya Ustun-Alkan5
1Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran.
Abstract:
RON (Recepteur d'Origine Nantais) tyrosine kinase receptor is a promising target for therapeutic intervention in cancer therapy. The aim of this work was identification of RON-binding peptides using phage display and computational modeling their mode of binding. A 12-mer peptide phage library was utilized to perform biopanning against RON. The RON-binding ability of the selected peptide-displaying phage and their possible binding sites were examined by ELISA. Binding modes and affinities were also predicted by docking and molecular dynamics (MD) simulation. The results of ELISA experiment showed that P6 peptide displaying phage has higher affinity for RON compared to others and its binding site is located out of ligand binding site. Docking and MD simulation results also indicated higher affinity of P6 to RON as well as its exosite-binding feature. Taken together, our data suggest a capacity for P6 peptide (FEHSLYKEMTHL) to be utilized as RON binding agent, and hence be used for various purposes, including design of drug delivery systems for transferring cytotoxic agents to RON-positive cancer cells, interfering with RON signaling, peptidomimetics design, and diagnostic imaging.
Insights
Researchers identified a novel peptide, P6 (FEHSLYKEMTHL), that binds to the RON receptor tyrosine kinase. This peptide shows potential for cancer therapy applications, including drug delivery and diagnostics.
Area of Science:
- Biochemistry
- Molecular Biology
- Computational Chemistry
Background:
- The RON (Recepteur d'Origine Nantais) receptor tyrosine kinase is a significant target in cancer therapy.
- Developing specific agents to target RON is crucial for advancing cancer treatment strategies.
Purpose of the Study:
- To identify peptides that bind to the RON receptor using phage display.
- To computationally model the binding mode and affinity of identified peptides to RON.
Main Methods:
- Biopanning a 12-mer peptide phage library against the RON receptor.
- Enzyme-linked immunosorbent assay (ELISA) to assess binding affinity and sites.
- Molecular docking and molecular dynamics (MD) simulations to predict binding modes and affinities.
Main Results:
- The P6 peptide-displaying phage exhibited higher affinity for RON compared to other selected phages.
- ELISA and computational analyses indicated that P6 binds to an exosite on RON, distinct from the ligand-binding site.
- Docking and MD simulations confirmed the high affinity and exosite-binding nature of the P6 peptide.
Conclusions:
- The P6 peptide (FEHSLYKEMTHL) demonstrates significant capacity as a RON-binding agent.
- P6 holds potential for applications in drug delivery systems targeting RON-positive cancer cells.
- Further applications include interfering with RON signaling, peptidomimetics design, and diagnostic imaging.
