Natural ligand binding and transfer from liver fatty acid binding protein (LFABP) to membranes

Eduardo De Geronimo, Robert M. Hagan, David C. Wilton, Betina Corsico

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

Liver fatty acid-binding protein (LFABP) is distinctive among fatty acid-binding proteins because it binds more than one molecule of long-chain fatty acid and a variety of diverse ligands. Also, the transfer of fluorescent fatty acid analogues to model membranes under physiological ionic strength follows a different mechanism compared to most of the members of this family of intracellular lipid binding proteins. Tryptophan insertion mutants sensitive to ligand binding have allowed us to directly measure the binding affinity, ligand partitioning and transfer to model membranes of natural ligands. Binding of fatty acids shows a cooperative mechanism, while acyl-CoAs binding presents a hyperbolic behavior. Saturated fatty acids seem to have a stronger partition to protein vs. membranes, compared to unsaturated fatty acids. Natural ligand transfer rates are more than 200-fold higher compared to fluorescently-labeled analogues. Interestingly, oleoyl-CoA presents a markedly different transfer behavior compared to the rest of the ligands tested, probably indicating the possibility of specific targeting of ligands to different metabolic fates. (C) 2010 Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)1082-1089
Number of pages8
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume1801
Issue number9
DOIs
Publication statusPublished - Sept 2010

Keywords

  • Fatty acid
  • Acyl-CoA
  • Lipid binding protein
  • Lipid transfer
  • Enterocyte
  • Lipid metabolism
  • ACTIVATED RECEPTOR-ALPHA
  • COLLISION-MEDIATED TRANSFER
  • ACYL-COA
  • PHOSPHOLIPID-MEMBRANES
  • HELICAL DOMAIN
  • DIFFERENT MECHANISMS
  • HEART
  • LYSOPHOSPHOLIPIDS
  • EXPRESSION
  • ADIPOCYTE

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