Fulvio Perrella1, Federico Coppola1, Alessio Petrone1, Chiara Platella1, Daniela Montesarchio1, Annarita Stringaro2, Giampietro Ravagnan3, Maria Pia Fuggetta3, Nadia Rega1,4, Domenica Musumeci1,5. 1. Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy. 2. National Center for Drug Research and Evaluation, Italian National Institute of Health, 00161 Rome, Italy. 3. Institute of Translational Pharmacology, Consiglio Nazionale delle Ricerche, 00133 Rome, Italy. 4. Centro di Ricerca Interdipartimentale sui Biomateriali, University of Naples Federico II, Piazzale Tecchio, 80125 Naples, Italy. 5. Institute of Biostructures and Bioimages, Consiglio Nazionale delle Ricerche, 80134 Naples, Italy.
Abstract
In the search for new therapeutic strategies to contrast SARS-CoV-2, we here studied the interaction of polydatin (PD) and resveratrol (RESV)-two natural stilbene polyphenols with manifold, well known biological activities-with Spike, the viral protein essential for virus entry into host cells, and ACE2, the angiotensin-converting enzyme present on the surface of multiple cell types (including respiratory epithelial cells) which is the main host receptor for Spike binding. Molecular Docking simulations evidenced that both compounds can bind Spike, ACE2 and the ACE2:Spike complex with good affinity, although the interaction of PD appears stronger than that of RESV on all the investigated targets. Preliminary biochemical assays revealed a significant inhibitory activity of the ACE2:Spike recognition with a dose-response effect only in the case of PD.
In the search for new therapeutic strategies to contrast SARS-CoV-2, we here studied the interaction of n class="Chemical">polydatin (PD) and resveratrol (RESV)-two natural stilbene polyphenols with manifold, well known biological activities-with Spike, the viral protein essential for virus entry into host cells, and ACE2, the angiotensin-converting enzyme present on the surface of multiple cell types (including respiratory epithelial cells) which is the main host receptor for Spike binding. Molecular Docking simulations evidenced that both compounds can bind Spike, ACE2 and the ACE2:Spike complex with good affinity, although the interaction of PD appears stronger than that of RESV on all the investigated targets. Preliminary biochemical assays revealed a significant inhibitory activity of the ACE2:Spike recognition with a dose-response effect only in the case of PD.