Abstract
Neuropilin-1 (NRP1) is a surface glycoprotein originally found to play a role in neuronal adhesion. It has since been discovered that NRP1 is involved in vascular development, as well as tumorigenesis. NRP1 has been previously shown to exist in a monomer-dimer equilibrium in the plasma membrane, in the presence of vascular endothelial growth factor (VEGF). With the addition of vascular endothelial growth factor receptor 2 (VEGFR2), NRP1 can also form heterodimers in the presence or absence of VEGF. The aim of my project is to further probe NRP1 homo-interactions and hetero-interactions with VEGFR2 in the presence and absence of VEGFA-165, using the number and brightness fluorescence fluctuation method (N&B). Using N&B, I hope to quantify the oligomer size of NRP1 under different conditions.
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