A perfect fit: The nanomolar affinity of a diketopiperazine-derived cyclic RGD-peptidomimetic for the integrin alpha-v-beta-3 receptor can be attributed to its high structural pre-organization. The trans-diketopiperazine scaffold induces an extended RGD disposition permitting all important interactions with the extracellular domain of the alpha-v-beta-3 integrin. The metal ion in the metal-ion-dependent adhesion site region is represented by a magenta sphere.
Cyclic RGD-Peptidomimetics Containing Bifunctional Diketopiperazine Scaffolds as New Potent Integrin Ligands / A.S.M. Ressurreição, A. Vidu, M. Civera, L. Belvisi, D. Potenza, L. Manzoni, S. Ongeri, C.M.A. Gennari, U. Piarulli. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 15:45(2009), pp. 12184-12188.
Cyclic RGD-Peptidomimetics Containing Bifunctional Diketopiperazine Scaffolds as New Potent Integrin Ligands
M. Civera;L. Belvisi;D. Potenza;C.M.A. GennariPenultimo
;
2009
Abstract
A perfect fit: The nanomolar affinity of a diketopiperazine-derived cyclic RGD-peptidomimetic for the integrin alpha-v-beta-3 receptor can be attributed to its high structural pre-organization. The trans-diketopiperazine scaffold induces an extended RGD disposition permitting all important interactions with the extracellular domain of the alpha-v-beta-3 integrin. The metal ion in the metal-ion-dependent adhesion site region is represented by a magenta sphere.
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