Investigation on the sucrose binding pocket of HIV-1 Integrase by molecular dynamics and synergy experiments
- Author(s)
- Cristina Tintori, Francesca Esposito, Francesca Morreale, Riccardo Martini, Enzo Tramontano, Maurizio Botta
- Abstract
Enzymes whose catalytic activity depends on multimeric assembly are targets for inhibitors that perturb the interactions between the protein subunits such as the HIV-1 Integrase (IN). Sucrose has been recently crystallized in complex with IN revealing an allosteric binding pocket at the monomer-monomer interface. Herein, molecular dynamics were applied to theoretically test the effect of this small ligand on IN. As a result, such a compound increases the mutual free energy of binding between the two interacting monomers. Biological experiments confirmed the computational forecast.
- Organisation(s)
- External organisation(s)
- Università Degli Studi di Siena, Università degli Studi di Cagliari, Università degli Studi di Messina, Temple University, Philadelphia
- Journal
- Bioorganic & Medicinal Chemistry Letters
- Volume
- 25
- Pages
- 3013-3016
- No. of pages
- 4
- ISSN
- 0960-894X
- DOI
- https://doi.org/10.1016/j.bmcl.2015.05.011
- Publication date
- 08-2015
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 301207 Pharmaceutical chemistry
- Keywords
- ASJC Scopus subject areas
- Drug Discovery, Molecular Medicine, Molecular Biology, Biochemistry, Clinical Biochemistry, Pharmaceutical Science, Organic Chemistry
- Sustainable Development Goals
- SDG 3 - Good Health and Well-being
- Portal url
- https://ucris.univie.ac.at/portal/en/publications/investigation-on-the-sucrose-binding-pocket-of-hiv1-integrase-by-molecular-dynamics-and-synergy-experiments(505e2fc8-73c4-4601-b480-979ed3a15ccd).html