Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorDantas, Diego de Sousa-
dc.contributor.authorOliveira, Jonas Ivan Nobre-
dc.contributor.authorLima Neto, José Xavier de-
dc.contributor.authorCosta, Roner Ferreira da-
dc.contributor.authorBezerra, Eveline Matias-
dc.contributor.authorFreire, Valder Nogueira-
dc.contributor.authorCaetano, Ewerton Wagner Santos-
dc.contributor.authorFulco, Umberto Laino-
dc.contributor.authorAlbuquerque, Eudenilson Lins de-
dc.identifier.citationDANTAS, D. S.; OLIVEIRA, J. I. N.; LIMA NETO, J. X.; COSTA, R. F.; BEZERRA, E. M.; FREIRE, V. N.; CAETANO, E. W. S.; FULCO, U. L.; ALBUQUERQUE, E. L.pt_BR
dc.description.abstractThe binding of the nonsteroidal anti-inflammatory drug ibuprofen (IBU) to human serum albumin (HSA) is investigated using density functional theory (DFT) calculations within a fragmentation strategy. Crystallographic data for the IBU–HSA supramolecular complex shows that the ligand is confined to a large cavity at the subdomain IIIA and at the interface between the subdomains IIA and IIB, whose binding sites are FA3/FA4 and FA6, respectively. The interaction energy between the IBU molecule and each amino acid residue of these HSA binding pockets was calculated using the Molecular Fractionation with Conjugate Caps (MFCC) approach employing a dispersion corrected exchange–correlation functional. Our investigation shows that the total interaction energy of IBU bound to HSA at binding sites of the fatty acids FA3/FA4 (FA6) converges only for a pocket radius of at least 8.5 °A, mainly due to the action of residues Arg410, Lys414 and Ser489 (Lys351, Ser480 and Leu481) and residues in nonhydrophobic domains, namely Ile388, Phe395, Phe403, Leu407, Leu430, Val433, and Leu453 (Phe206, Ala210, Ala213, and Leu327), which is unusual. Our simulations are valuable for a better understanding of the binding mechanism of IBU to albumin and can lead to the rational design and the development of novel IBU-derived drugs with improved potency.pt_BR
dc.publisherRSC Advancespt_BR
dc.subjectTeoria da densidade funcional (DFT)pt_BR
dc.subjectAlbumina sérica humanapt_BR
dc.titleQuantum molecular modelling of ibuprofen bound to human serum albuminpt_BR
dc.typeArtigo de Periódicopt_BR
Appears in Collections:DFI - Artigos publicados em revista científica

Files in This Item:
File Description SizeFormat 
2015_art_dsdantas.pdf2,71 MBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.