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

Antonio      Carrieri; Enza      Lacivita; Benny   Danilo   Belviso; Rocco      Caliandro; Piero      Mastrorilli; Vito      Gallo; Mauro      Niso; Marcello      Leopoldo

doi:10.2174/1568026617666161104102459

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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DOI https://dx.doi.org/10.2174/1568026617666161104102459	Print ISSN 1568-0266
Publisher Name Bentham Science Publisher	Online ISSN 1873-4294

Current Topics in Medicinal Chemistry

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

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