Design, synthesis and characterization of helical oligopeptides inhibiting the VEGF/VEGFR protein-protein interaction
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Data di Pubblicazione:
2015
Citazione:
Design, synthesis and characterization of helical oligopeptides inhibiting the VEGF/VEGFR protein-protein interaction / L. Belvisi, G. Bocchinfuso, S. Raniolo, A. Palleschi, M. De Zotti, G. Panighel, F. Formaggio, D. Arosio, U. Piarulli, S. Zanella, L. Pignataro, C. Gennari, L. Stella. ((Intervento presentato al 36. convegno Convegno della Divisione di Chimica Organica della Società Chimica Italiana tenutosi a Bologna nel 2015.
Abstract:
Protein-protein interactions modulate most biological processes, but their inhibition by small organic molecules is challenging, due to the large interacting protein interfaces. One example is provided by the association between vascular endothelial growth factors (VEGFs) and their receptors (VEGFRs). It is crucial in regulating angiogenesis and therefore constitutes a key target in cancer therapy. Oligopeptides mimicking a VEGF interface helix represent a promising strategy to inhibit this interaction.1
Here we report in silico design, synthesis, structural and functional characterization of several short peptides (9-15 residues) targeting VEGFRs. In particular, we exploited the known helix-inducing capabilities of Cα-tetrasubstituted α amino acids to stabilize the secondary structure of our peptides.2
We gratefully acknowledge MIUR for financial support (PRIN project 2010NRREPL: Synthesis and biomedical applications of tumor-targeting peptidomimetics).
Tipologia IRIS:
14 - Intervento a convegno non pubblicato
Elenco autori:
L. Belvisi, G. Bocchinfuso, S. Raniolo, A. Palleschi, M. De Zotti, G. Panighel, F. Formaggio, D. Arosio, U. Piarulli, S. Zanella, L. Pignataro, C. Gennari, L. Stella
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