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- W2772067201 abstract "Neuropilin-1 (NRP1), which functions as a coreceptor for vascular endothelial growth factor (VEGF) and is implicated in vascular permeability and tumorigenesis, has been targeted by peptides that specifically bind to the VEGF-binding region on NRP1. Like natural VEGF ligands, all known peptides with NRP1-binding activity bind only through a carboxy (C)-terminal R/K-x-x-R/K sequence motif (x stands for any amino acids); this strict requirement is called the C-end rule (CendR). Here, we report immunoglobulin Fc-fused NRP1-specific peptides deviating from CendR. We screened a yeast surface-displayed Fc-fused non-CendR peptide library against NRP1 and isolated Fc-V12, wherein V12 peptide comprising 12 amino acids has a PPRV sequence at its C-terminal end. Although Fc-V12 lacked the CendR motif, it showed selective binding to the VEGF-binding region of NRP1 and triggered cellular internalization of NRP1, which resulted in enhanced extravasation into tumor tissues and tumor tissue penetration of the Fc-fused pe..." @default.
- W2772067201 created "2017-12-22" @default.
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- W2772067201 date "2017-12-21" @default.
- W2772067201 modified "2023-10-12" @default.
- W2772067201 title "Immunoglobulin Fc-Fused Peptide without C-Terminal Arg or Lys Residue Augments Neuropilin-1-Dependent Tumor Vascular Permeability" @default.
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- W2772067201 doi "https://doi.org/10.1021/acs.molpharmaceut.7b00761" @default.
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