caa a22 4500 467938938 CHVBK 20180406153006.0 cr unu---uuuuu 170328e20060501xx s 000 0 eng 10.1007/s10822-006-9055-1 doi (NATIONALLICENCE)springer-10.1007/s10822-006-9055-1 Pharmacophore model for bile acids recognition by the FPR receptor [Elektronische Daten] [Cristina Ferrari, Antonio Macchiarulo, Gabriele Costantino, Roberto Pellicciari] Formyl-peptide receptors (FPRs) belong to the family A of the G-protein coupled receptor superfamily and include three subtypes: FPR, FPR-like-1 and FPR-like-2. They have been involved in the control of␣many inflammatory processes promoting the recruitment and infiltration of leukocytes in regions of inflammation through the molecular recognition of chemotactic factors. A large number of structurally diverse chemotypes modulate the activity of FPRs. Newly identified antagonists include bile acids deoxycholic acid (DCA) and chenodeoxycholic acid (CDCA). The molecular recognition of these compounds at FPR receptor was computationally investigated using both ligand- and structure-based approaches. Our findings suggest that all antagonists bind at the first third of the seven helical bundles. A closer inspection of bile acid interaction reveals a number of unexploited anchor points in the binding site that may be used to aid the design of new potent and selective bile acids derivatives at FPR. Springer Science+Business Media B.V., 2006 Antagonists nationallicence Bile acids nationallicence Formyl-peptide receptors nationallicence G-protein coupled receptors nationallicence Molecular modeling nationallicence Molecular recognition nationallicence Pharmacophore nationallicence Rational drug design nationallicence GPCR : G protein-coupled receptor nationallicence FPR : formylpeptide receptor nationallicence FPRL-1 : formyl peptide receptor like type-1 nationallicence FPRL-2 : formyl peptide receptor like type-2 nationallicence DCA : deoxycholic acid nationallicence CDCA : chenodeoxycholic acid nationallicence Ferrari Cristina Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut Macchiarulo Antonio Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut Costantino Gabriele Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut Pellicciari Roberto Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 20/5(2006-05-01), 295-303 0920-654X 20:5<295 2006 20 10822 https://doi.org/10.1007/s10822-006-9055-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10822-006-9055-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ferrari Cristina Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut NATIONALLICENCE 700 1- Macchiarulo Antonio Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut NATIONALLICENCE 700 1- Costantino Gabriele Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut NATIONALLICENCE 700 1- Pellicciari Roberto Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, via del Liceo 1, 06127, Perugia, Italy aut NATIONALLICENCE 773 0- Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 20/5(2006-05-01), 295-303 0920-654X 20:5<295 2006 20 10822 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer