Cyclic RGD‐Peptidomimetics Containing Bifunctional Diketopiperazine Scaffolds as New Potent Integrin Ligands | Zendy

da Ressurreição Ana Sofia M. | Zendy; Vidu Anamaria | Zendy; Civera Monica | Zendy; Belvisi Laura | Zendy; Potenza Donatella | Zendy; Manzoni Leonardo | Zendy; Ongeri Sandrine | Zendy; Gennari Cesare | Zendy; Piarulli Umberto | Zendy

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Cyclic RGD‐Peptidomimetics Containing Bifunctional Diketopiperazine Scaffolds as New Potent Integrin Ligands

Author(s) -

da Ressurreição Ana Sofia M.,

Vidu Anamaria,

Civera Monica,

Belvisi Laura,

Potenza Donatella,

Manzoni Leonardo,

Ongeri Sandrine,

Gennari Cesare,

Piarulli Umberto

Publication year - 2009

Publication title -

chemistry – a european journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.687

H-Index - 242

eISSN - 1521-3765

pISSN - 0947-6539

DOI - 10.1002/chem.200902398

Subject(s) - peptidomimetic , integrin , chemistry , scaffold , stereochemistry , bifunctional , computational biology , domain (mathematical analysis) , combinatorial chemistry , receptor , computer science , biochemistry , biology , peptide , mathematics , database , mathematical analysis , catalysis

A perfect fit : The nanomolar affinity of a diketopiperazine‐derived cyclic RGD‐peptidomimetic for the integrin α v β 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 α v β 3 integrin. The metal ion in the metal‐ion‐dependent adhesion site region is represented by a magenta sphere.

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