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- W2014764992 abstract "The design, synthesis, conformational studies and binding affinity for VEGFR-1 receptors of a collection of linear and cyclic peptide analogues of the β-hairpin fragment VEGF81–91 are described. Cyclic 11-mer peptide derivatives were prepared from linear precursors with conveniently located Cys, Asp or Dap residues, by the formation of disulfide and amide bridges, using solid-phase synthesis. Molecular modelling studies indicated a tendency to be structured around the central β-turn of the VEGF81–91 β-hairpin in most synthesized cyclic compounds. This structural behavior was confirmed by NMR conformational analysis. The NHCO cyclic derivative 7 showed significant affinity for VEGFR-1, slightly higher than the native linear fragment, thus supporting the design of mimics of this fragment as a valid approach to disrupt the VEGF/VEGFR-1 interaction." @default.
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- W2014764992 date "2011-12-01" @default.
- W2014764992 modified "2023-10-18" @default.
- W2014764992 title "Disulfide and amide-bridged cyclic peptide analogues of the VEGF81–91 fragment: Synthesis, conformational analysis and biological evaluation" @default.
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- W2014764992 doi "https://doi.org/10.1016/j.bmc.2011.10.032" @default.
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