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2-domain soluble FMS-like tyrosine kinase-1 (2d-sFlt-1) is a novel recombinant truncated form of soluble FMS-like tyrosine kinase-1 (sFlt-1/VEGFR1) containing only the first two extracellular domains. Developed by researchers at the University of Mysore, 2d-sFlt-1 acts as a decoy receptor that binds to vascular endothelial growth factor (VEGF), thereby inhibiting VEGF-mediated angiogenesis and tumor-endothelial crosstalk. In preclinical studies, 2d-sFlt-1 has demonstrated synergistic anti-tumor, anti-angiogenic, and anti-metastatic effects when combined with paclitaxel in three-dimensional (3D) multicellular spheroid models of breast cancer, particularly triple-negative breast cancer (TNBC). It has also been investigated for its potential to bind the SARS-CoV-2 spike receptor-binding domain (RBD).
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