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Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
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Assessment of Phage-Displayed Peptides Targeting Cancer Cell Surface Proteins: A Comprehensive Molecular Docking
Verónica Quilumba-Dutan1, Clara Carreón-Álvarez2,3, Víctor Sanabria-Ayala2,4
1Advanced Materials Department, Instituto Potosino de Investigación Científica y Tecnológica, San Luis Potosí, Mexico.
Abstract:
Peptides binding overexpressed breast and cervical cancer cell surface proteins can be isolated by phage display technology, and their affinity to their potential receptors can be assessed by molecular docking. We isolated 44 phage clones displaying dodecapeptides with high affinity to HeLa cervical cancer and MDA-MB-231 (MDA) breast cancer cells by repeated biopanning of an MK13 phage library and explored their affinity to specific proteins by molecular docking. Six peptides appeared repeatedly during biopanning: two with affinity to HeLa (H5/H21), and four with affinity to MDA cells (M3/M7/M15/M17). Peptide pairs M3/H5 and H1/M17 had affinity to both cell lines. A systematic review identified Annexin A2, EGFR, CD44, CD146, and Integrin alpha V as potential protein targets in HeLa cells, and Vimentin, Galectin-1, and Annexins A1 and A5 in MDA cells. Via virtual screening, we selected six peptides with the highest total docking scores: H1 (-916.32), H6 (-979.21), H19 (-1093.24), M6 (-732.21), M16 (-745.5), and M19 (-739.64), and identified that docking scores were strengthened by the protein type, the interacting amino acid side chains, and the polarity of peptides. This approach facilitates the selection of relevant peptides that could be further explored for active targeting in cancer diagnosis and treatment.
Insights
Researchers identified specific peptides that bind to breast and cervical cancer cells using phage display and molecular docking. These peptides show potential for targeted cancer therapy and diagnosis.
Area of Science:
- Biotechnology
- Oncology
- Molecular Biology
Background:
- Cancer cell surface proteins are targets for diagnosis and therapy.
- Phage display is a powerful tool for identifying binding ligands.
- Molecular docking can predict and assess ligand-receptor interactions.
Purpose of the Study:
- To isolate and characterize peptides that bind to breast and cervical cancer cells.
- To evaluate the affinity of these peptides to specific cancer cell surface proteins.
- To explore the potential of these peptides in targeted cancer therapy.
Main Methods:
- Phage display biopanning using HeLa (cervical) and MDA-MB-231 (breast) cancer cells.
- Systematic review to identify potential protein targets.
- Molecular docking simulations to assess peptide-protein interactions and binding affinity.
Main Results:
- 44 phage clones displaying high-affinity dodecapeptides were isolated.
- Six peptides (H5/H21 for HeLa, M3/M7/M15/M17 for MDA) were repeatedly identified.
- Identified potential protein targets including Annexin A2, EGFR, CD44, CD146, Integrin alpha V, Vimentin, Galectin-1, Annexins A1 and A5.
- Selected six peptides (H1, H6, H19, M6, M16, M19) with the highest docking scores, indicating strong binding affinity.
Conclusions:
- Phage display and molecular docking effectively identified high-affinity peptides for cancer cells.
- These peptides show promise for developing targeted cancer diagnostic and therapeutic agents.
- Further exploration of these peptides could lead to novel cancer treatment strategies.
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