Angiogenesis is a key target in cancer therapy. With the aim at regulating this process, we recently designed, synthesized and investigated an array of peptides based on the IDNEWRKTQ sequence of the vascular endothelial growth factor (VEGF)-C. The new peptides were optimized to increase both helix stability and binding affinity towards the VEGF receptors. In particular, we exploited the known helix-inducing capabilities of Cα-tetrasubstituted -amino acids to stabilize the secondary structure of our peptides. In addition, we inserted Trp residues at appropriate positions to enhance the binding affinity. The conformational preferences of our peptides were investigated by CD and 2D-NMR in aqueous solution. Data analysis confirmed the onset of helical structures. Interestingly, we observed that the absorption bands in the near-UV of the indole (Trp) chromophore constitute a reliable probe to assess the conformational stability of our helical peptides. In this presentation we will correlate this CD feature to the information extracted from the NMR analysis.

CD spectra in the near-UV of VEGF-C analogs to assess peptide conformational stability / F. Formaggio, M. De Zotti, G. Bocchinfuso, A. Palleschi, D. Arosio, U. Piarulli, S. Zanella, L. Pignataro, L. Belvisi, C. Gennari, L. Stella. ((Intervento presentato al convegno Diagnostic and therapeutic applications of integrin-targeted peptidomimetic ligands and conjugates tenutosi a Bologna nel 2016.

CD spectra in the near-UV of VEGF-C analogs to assess peptide conformational stability

S. Zanella;L. Pignataro;L. Belvisi;C. Gennari;
2016-02-15

Abstract

Angiogenesis is a key target in cancer therapy. With the aim at regulating this process, we recently designed, synthesized and investigated an array of peptides based on the IDNEWRKTQ sequence of the vascular endothelial growth factor (VEGF)-C. The new peptides were optimized to increase both helix stability and binding affinity towards the VEGF receptors. In particular, we exploited the known helix-inducing capabilities of Cα-tetrasubstituted -amino acids to stabilize the secondary structure of our peptides. In addition, we inserted Trp residues at appropriate positions to enhance the binding affinity. The conformational preferences of our peptides were investigated by CD and 2D-NMR in aqueous solution. Data analysis confirmed the onset of helical structures. Interestingly, we observed that the absorption bands in the near-UV of the indole (Trp) chromophore constitute a reliable probe to assess the conformational stability of our helical peptides. In this presentation we will correlate this CD feature to the information extracted from the NMR analysis.
Settore CHIM/06 - Chimica Organica
CD spectra in the near-UV of VEGF-C analogs to assess peptide conformational stability / F. Formaggio, M. De Zotti, G. Bocchinfuso, A. Palleschi, D. Arosio, U. Piarulli, S. Zanella, L. Pignataro, L. Belvisi, C. Gennari, L. Stella. ((Intervento presentato al convegno Diagnostic and therapeutic applications of integrin-targeted peptidomimetic ligands and conjugates tenutosi a Bologna nel 2016.
Conference Object
File in questo prodotto:
Non ci sono file associati a questo prodotto.
Pubblicazioni consigliate

Caricamento pubblicazioni consigliate

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/386926
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact