کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1362506 | 981489 | 2010 | 14 صفحه PDF | دانلود رایگان |
Neuropilin-1 (NRP-1) is a co-receptor of VEGFR165 and molecules interfering with VEGF165 binding to NRP-1 seem to be promising candidates as new angiogenesis modulators. Based on the minimal four amino acid sequence of peptidic ligands known to bind NRP-1, we describe here the design, synthesis and biological evaluation of series of original sugar-based peptidomimetics using a C-glycosyl compound, derived from d-gulonolactone, as a scaffold, which was functionalized with side chains of the amino-acids arginine, and tryptophane or threonine. At 100 μM, all compounds exhibited a weak affinity for NRP-1, the most efficient being the bis-guanidinylated compound 32 (IC50 = 92 μM) which could be considered as a new NRP-1 non-peptidic ligand.
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Journal: Bioorganic & Medicinal Chemistry - Volume 18, Issue 9, 1 May 2010, Pages 3285–3298