Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 25, Issue 2, Pages 597-602Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2016.11.024
Keywords
Angiogenesis; VEGF(165); NRP-1; A7R; Cyclic peptides; Docking analysis
Funding
- National Science Centre (NCN) [N204 350940]
- EU from the European Regional Development Fund
- EU program
- University of Warsaw for young researchers [120000-501/86-DSM-110200]
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Inhibition of angiogenesis is one of the most promising approaches in anticancer therapy. It was recently suggested that Neuropilin-1 (NRP-1) in tumour cells may serve as a separate receptor for Vascular Endothelial Growth Factor-165 (VEGF(165)) which is one of the main pro-angiogenic agents in the organism. Therefore molecules inhibiting VEGF(165) binding to NRP-1 could be potential candidates for new antiangiogenic and anticancer drugs. Here we present a structure-activity relationship study of the peptide H-c[Lys-Pro-Glu]-Arg-OH which showed high inhibitory effect on VEGF(165)/NRP-1 binding (IC50 = 0.18 mu M) in our previous study. We report the design, synthesis, in vitro assays and docking analysis of four small cyclic peptides (14-,15-membered ring) and one bigger cyclic compound (30-membered ring). Our study shows that both the ring size and configuration of amino acid residues present in the structure are crucial for high inhibitory effect. (C) 2016 Elsevier Ltd. All rights reserved.
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