Dynamics of ligand and nanobody binding at CXCR4/EGFR complexesTools Comez, Dehan (2025) Dynamics of ligand and nanobody binding at CXCR4/EGFR complexes. PhD thesis, University of Nottingham.
AbstractUnderstanding the cell signalling of cancer has the potential to impact the development of anti-cancer therapeutics. The dimerisation of cell membrane receptors is one of the key modulators of cancer cell signalling. G-protein coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs) are two prominent receptor families regulating various cellular processes in normal physiology and cancer progression. The abnormalities in membrane receptors, such as mutations, overexpression or enhanced receptor-receptor interaction are relevant for many cancer types. CXCR4 is significantly upregulated in numerous cancers, which correlates to cancer progression. Epidermal growth factor receptor (EGFR) is one of the major growth hormone receptors critical to various cancers, promoting cancer progression, proliferation, survival, and metastasis. This thesis aimed to elucidate the dynamics of CXCR4 and EGFR complexes. NanoLuciferase Bioluminescence Resonance Energy Transfer (NanoBRET) was used to quantify interacting characteristics of CXCR4/EGFR dimerisation with NanoLuciferase and fluorophore tags on receptors. Proximity Ligation Assay (PLA) was also used to detect endogenously expressed CXCR4/EGFR dimers on HeLa cells with receptor specific nanobodies conjugated to oligonucleotides.
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