Structure-function analysis of the antiangiogenic ATWLPPR peptide inhibiting VEGF(165) binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex.

@article{Starzec2007StructurefunctionAO,
  title={Structure-function analysis of the antiangiogenic ATWLPPR peptide inhibiting VEGF(165) binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex.},
  author={Anna Starzec and Patrick Ladam and Roger Vassy and Sabah Badache and Nadia Bouchemal and Alda Navaza and Catherine Herv{\'e} du Penhoat and G{\'e}rard Yves Perret},
  journal={Peptides},
  year={2007},
  volume={28 12},
  pages={2397-402}
}
Heptapeptide ATWLPPR (A7R), identified in our laboratory by screening a mutated phage library, was shown to bind specifically to neuropilin-1 (NRP-1) and then to selectively inhibit VEGF(165) binding to this receptor. In vivo, treatment with A7R resulted in decreasing breast cancer angiogenesis and growth. The present work is focused on structural characterization of A7R. Analogs of the peptide, obtained by substitution of each amino acid with alanine (alanine-scanning) or by amino acid… CONTINUE READING