Structural Determinants in the Binding of BB2 Receptor Ligands: In Silico, X-Ray and NMR Studies in PD176252 Analogues

Author(s): Antonio Carrieri*, Enza Lacivita, Benny Danilo Belviso, Rocco Caliandro, Piero Mastrorilli, Vito Gallo, Mauro Niso, Marcello Leopoldo

Journal Name: Current Topics in Medicinal Chemistry

Volume 17 , Issue 14 , 2017

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Graphical Abstract:


Background: The mammalian bombesin receptor family comprises three G proteincoupled receptors: the neuromedin B receptor, the gastrin-releasing peptide receptor (BB2), and the bombesin receptor subtype 3. BB2 receptor plays a role in gastrointestinal functions; however, at present the role of this subtype in physiological and pathological conditions is unknown due to the lack of specific binders for all subclasses of bombesin receptors.

Results: Here, we present a study focused on the properties of the peptoid bombesin antagonist called PD176252, and other structural analogues with the aim to elucidate causes of their different affinity towards the BB2 receptor.

Conclusion: By means of computational techniques, based on QSAR, docking and homology building, supported by experimental data (X-ray diffraction and NMR spectroscopy) fresh insights on binding modes of this class of biological targets were achieved.

Keywords: PD176252, Bombesin receptor, QSAR, Docking, X-ray, NOESY.

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Article Details

Year: 2017
Published on: 05 April, 2017
Page: [1599 - 1610]
Pages: 12
DOI: 10.2174/1568026617666161104102459
Price: $65

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