CATALOGO DEI PRODOTTI DELLA RICERCA
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishFatty acid binding proteins (FABPs) act as intracellular carriers of lipid molecules, and play a role in global metabolism regulation. Liver FABP (L-FABP) is characterized by high versatility in terms of ligand binding capabilities.[1] Indeed, both long chain fatty acids as well as bulkier ligands can be accommodated into the protein’s large internal cavity. The involvement of L-FABP in the transport of bile salts has been postulated but scarcely investigated.[2] This hypothesis is further supported by the realization that L-BABP (a type 2 intracellular lipid binding protein bile-salt carrier) is absent in mammals. We have used a variety of NMR experiments, as well as steady-state fluorescence spectroscopy, and mass spectrometry to gain insight, at molecular and atomic level, into the interactions established by human L-FABP with a pool of bile acids [3, 4], contributing to improve our understanding of the binding specificity for this important class of cholesterol-derived metabolites. An extensive comparison among L-FABP alone, in complex with bile acids, and in complex with oleate, has been performed in order to investigate the distinctive features of L-FABP binding promiscuity.[3] NMR relaxation experiments on different timescales suggest that human L-FABP is poorly selective in terms of ligand binding and a functional role is played by its internal dynamics. Taken together our findings expand the current knowledge about ligand recognition by L-FABP with implications in the intracellular transport of bile acids in physiological and pathological states.
| Titolo: | Understanding promiscuous and selective ligand binding by liver FABP |
| Autori: | |
| Data di pubblicazione: | 2015 |
| Rivista: | |
| Abstract: | Fatty acid binding proteins (FABPs) act as intracellular carriers of lipid molecules, and play a role in global metabolism regulation. Liver FABP (L-FABP) is characterized by high versatility in terms of ligand binding capabilities.[1] Indeed, both long chain fatty acids as well as bulkier ligands can be accommodated into the protein’s large internal cavity. The involvement of L-FABP in the transport of bile salts has been postulated but scarcely investigated.[2] This hypothesis is further supported by the realization that L-BABP (a type 2 intracellular lipid binding protein bile-salt carrier) is absent in mammals. We have used a variety of NMR experiments, as well as steady-state fluorescence spectroscopy, and mass spectrometry to gain insight, at molecular and atomic level, into the interactions established by human L-FABP with a pool of bile acids [3, 4], contributing to improve our understanding of the binding specificity for this important class of cholesterol-derived metabolites. An extensive comparison among L-FABP alone, in complex with bile acids, and in complex with oleate, has been performed in order to investigate the distinctive features of L-FABP binding promiscuity.[3] NMR relaxation experiments on different timescales suggest that human L-FABP is poorly selective in terms of ligand binding and a functional role is played by its internal dynamics. Taken together our findings expand the current knowledge about ligand recognition by L-FABP with implications in the intracellular transport of bile acids in physiological and pathological states. |
| Handle: | http://hdl.handle.net/11562/932631 |
| Appare nelle tipologie: | 04.02 Abstract in Atti di convegno |
File in questo prodotto:
Copyright © 2021