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FasL-Ex4 is an experimental recombinant fusion protein consisting of the extracellular domain of Fas ligand (FasL) fused to exendin-4, a glucagon-like peptide-1 receptor (GLP-1R) agonist [512]. Developed by researchers at the University of Wuerzburg and the University of Giessen, the therapeutic candidate is designed to selectively target and destroy GLP-1R-expressing pancreatic beta-cells [512]. By binding to GLP-1R, the fusion protein is immobilized on the cell surface, allowing the FasL domain to locally activate the Fas receptor (CD95) and trigger extrinsic apoptosis [512]. This targeted approach is being investigated as a potential non-surgical treatment for insulinomas and disorders of pathological autonomic insulin secretion, such as nesidioblastosis (persistent hyperinsulinemic hypoglycemia of infancy) [512].
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