C-Glycosyl Compound

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Yves Chapleur - One of the best experts on this subject based on the ideXlab platform.

  • Sugar-based peptidomimetics as potential inhibitors of the vascular endothelium growth factor binding to neuropilin-1
    Bioorganic and Medicinal Chemistry, 2010
    Co-Authors: Alexandre Novoa, Nadia Pellegrini-moïse, Denise Bechet, Muriel Barberi-heyob, Yves Chapleur
    Abstract:

    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. © 2010 Elsevier Science. All rights reserved

Alexandre Novoa - One of the best experts on this subject based on the ideXlab platform.

  • Sugar-based peptidomimetics as potential inhibitors of the vascular endothelium growth factor binding to neuropilin-1
    Bioorganic and Medicinal Chemistry, 2010
    Co-Authors: Alexandre Novoa, Nadia Pellegrini-moïse, Denise Bechet, Muriel Barberi-heyob, Yves Chapleur
    Abstract:

    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. © 2010 Elsevier Science. All rights reserved

Nadia Pellegrini-moïse - One of the best experts on this subject based on the ideXlab platform.

  • Sugar-based peptidomimetics as potential inhibitors of the vascular endothelium growth factor binding to neuropilin-1
    Bioorganic and Medicinal Chemistry, 2010
    Co-Authors: Alexandre Novoa, Nadia Pellegrini-moïse, Denise Bechet, Muriel Barberi-heyob, Yves Chapleur
    Abstract:

    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. © 2010 Elsevier Science. All rights reserved

Denise Bechet - One of the best experts on this subject based on the ideXlab platform.

  • Sugar-based peptidomimetics as potential inhibitors of the vascular endothelium growth factor binding to neuropilin-1
    Bioorganic and Medicinal Chemistry, 2010
    Co-Authors: Alexandre Novoa, Nadia Pellegrini-moïse, Denise Bechet, Muriel Barberi-heyob, Yves Chapleur
    Abstract:

    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. © 2010 Elsevier Science. All rights reserved

Muriel Barberi-heyob - One of the best experts on this subject based on the ideXlab platform.

  • Sugar-based peptidomimetics as potential inhibitors of the vascular endothelium growth factor binding to neuropilin-1
    Bioorganic and Medicinal Chemistry, 2010
    Co-Authors: Alexandre Novoa, Nadia Pellegrini-moïse, Denise Bechet, Muriel Barberi-heyob, Yves Chapleur
    Abstract:

    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. © 2010 Elsevier Science. All rights reserved