title: Characterization of fatty acid binding and transfer from Δ98Δ, a functional all-β abridged form of IFABP.
abstract: Intestinal fatty acid binding protein (IFABP) is an intracellular lipid binding protein whose specific functions within the cell are still uncertain. An abbreviated version of IFABP encompassing residues 29-126, dubbed Δ98Δ is a stable product of limited proteolysis with clostripain of holo-IFABP. Cumulative evidence shows that Δ98Δ adopts a stable, monomeric and functional fold, with compact core and loose periphery. In agreement with previous results, this abridged variant indicates that the helical domain is-not necessary to preserve the general topology of IFABP's β-barrel and that the helix-turn-helix motif is a fundamental element of the portal region involved in ligand binding and protein-membrane interactions. Results presented here suggest that Δ98Δ binds fatty acids with affinities lower than IFABP but higher than those shown by previous helix-less variants, shows a 'diffusional' fatty acid transfer mechanism and it interacts with artificial membranes. This work highlights the importance of the β-barrel of IFABP for its specific functions.
authors.forename: Luciana Rodriguez
authors.initials: LR
authors.lastname: Sawicki
authors.forename: María Ximena
authors.initials: MX
authors.lastname: Guerbi
authors.forename: Lisandro Jorge
authors.initials: LJ
authors.lastname: Falomir Lockhart
authors.forename: Lucrecia María
authors.initials: LM
authors.lastname: Curto
authors.forename: José María
authors.initials: JM
authors.lastname: Delfino
authors.forename: Betina
authors.initials: B
authors.lastname: Córsico
authors.forename: Gisela Raquel
authors.initials: GR
authors.lastname: Franchini
mesh_terms: D020106:Acrylamide / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002498:Centrifugation; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D051381:Rats; D013050:Spectrometry, Fluorescence; D013395:Sucrose / Q000494:pharmacology; D013725:Terbium / Q000378:metabolism
chemical_list: D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D010743:Phospholipids; D020033:Protein Isoforms; D013725:Terbium; D020106:Acrylamide; D013395:Sucrose