Inhibition of the interaction between receptor neuropilin (NRP1) and vascular endothelial growth factor (VEGF-A) impacts tumour growth, and has been shown to synergistically enhance VEGF-A inhibitors.31 Using the crystal structures of NRP1/VEGF-A and an alanine scan of the identified binding site, the VEGF-A amino acids Tyr297, Trp301, Thr316, D320, S346, T349, Y353, K351 and Trp411 were highlighted as essential for binding. This evidence concerns the gene VEGFA and neoplasm.