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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.