Determination of the binding epitope of RGD-peptidomimetics to alphavbeta3 and alphaIIbbeta3 integrin-rich intact cells by NMR and computational studies (Articolo in rivista)

Type
Label
  • Determination of the binding epitope of RGD-peptidomimetics to alphavbeta3 and alphaIIbbeta3 integrin-rich intact cells by NMR and computational studies (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1039/c3ob40540k (literal)
Alternative label
  • Guzzetti, Ileana; Civera, Monica; Vasile, Francesca; Araldi, Elena M.; Belvisi, Laura; Gennari, Cesare; Potenza, Donatella; Fanelli, Roberto; Piarulli, Umberto (2013)
    Determination of the binding epitope of RGD-peptidomimetics to alphavbeta3 and alphaIIbbeta3 integrin-rich intact cells by NMR and computational studies
    in Organic & biomolecular chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Guzzetti, Ileana; Civera, Monica; Vasile, Francesca; Araldi, Elena M.; Belvisi, Laura; Gennari, Cesare; Potenza, Donatella; Fanelli, Roberto; Piarulli, Umberto (literal)
Pagina inizio
  • 3886 (literal)
Pagina fine
  • 3893 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 11 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 8 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 23 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • University of Milan; Consiglio Nazionale delle Ricerche (CNR); University of Insubria (literal)
Titolo
  • Determination of the binding epitope of RGD-peptidomimetics to alphavbeta3 and alphaIIbbeta3 integrin-rich intact cells by NMR and computational studies (literal)
Abstract
  • NMR experiments (transferred NOE and Saturation Transfer Difference) were used to shed light on the binding epitope of RGD peptidomimetics 1-3 with integrins alpha(v)beta(3) and alpha(IIb)beta(3), expressed on the membrane of ECV304 bladder cancer cells and human platelets, respectively. The NMR results were supported by docking calculations of 1-3 in the active sites of alpha(v)beta(3) and alpha(IIb)beta(3) integrin receptors and were compared to the results of competitive alpha(v)beta(3) receptor binding assays and competitive ECV304 cell adhesion experiments. While cis RGD ligand 1 interacts mainly with the a integrin subunit through its basic guanidine group, trans RGD ligands 2 and 3 are able to interact with both the alpha and beta integrin subunits via an electrostatic clamp. (literal)
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