Adipocyte fatty acid-binding protein

Interaction with phospholipid membranes and thermal stability studied by FTIR spectroscopy

Arne Gericke, Elizabeth R. Smith, David J. Moore, Richard Mendelsohn, Judith Storch

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Fatty acid-binding proteins (FABPs) found in many tissues constitute a family of low molecular weight proteins that are suggested to function as intracellular transporters of fatty acids. Studies of the transfer kinetics of fluorescent anthroyloxy-labeled long-chain fatty acids from FABP to model membranes led to the suggestion that the FABPs, typically considered to be cytosolic proteins, could nevertheless interact directly with membranes [Wootan, M. G., et al. (1993) Biochemistry 32, 8622-8627]. In the current study, the interaction of the adipocyte FABP (A-FABP) with vesicles of various phospholipids has been directly measured and confirmed with FTIR spectroscopy. The strength of this interaction was inferred from the lowering of the gel-liquid-crystal phase transition temperature as monitored from temperature-induced variations in the acyl chain CH2 stretching frequencies and from the intensities of the components of the CH2 wagging progressions. A-FABP interacts more strongly with anionic phospholipids (phosphatidylserine and cardiolipin) than with zwitterionic phosphatidylcholine. Unsaturation in the acyl chains leads to a greater reduction in T(m) (stronger lipid-protein interaction). In contrast, neutralization of A-FABP surface charges by acetylation considerably weakens the interaction. Comparison of the shifts in lipid melting temperatures with those induced by other proteins suggests that A-FABP behaves like a typical peripheral membrane protein. The degree of membrane interaction correlates directly with the rate of fatty acid transfer, suggesting that contact between A-FABP and membranes is functionally related to its fatty acid transport properties. As expected, the protein exhibits a predominantlyβ-sheet structure. It was found to aggregate with increasing temperature. With the exception of minor differences between the pure and lipid-associated A-FABP in the 1640-1660 cm-1 region, both the protein structure and thermal stability appeared essentially unchanged upon interaction with the lipid.

Original languageEnglish
Pages (from-to)8311-8317
Number of pages7
JournalBiochemistry
Volume36
Issue number27
DOIs
StatePublished - Jul 8 1997
Externally publishedYes

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Fatty Acid-Binding Proteins
Fourier Transform Infrared Spectroscopy
Adipocytes
Phospholipids
Spectrum Analysis
Thermodynamic stability
Hot Temperature
Spectroscopy
Membranes
Fatty Acids
Lipids
Proteins
Temperature
Liquid Crystals
Acetylation
Biochemistry
Cardiolipins
Transition Temperature
Phosphatidylserines
Phase Transition

ASJC Scopus subject areas

  • Biochemistry

Cite this

Adipocyte fatty acid-binding protein : Interaction with phospholipid membranes and thermal stability studied by FTIR spectroscopy. / Gericke, Arne; Smith, Elizabeth R.; Moore, David J.; Mendelsohn, Richard; Storch, Judith.

In: Biochemistry, Vol. 36, No. 27, 08.07.1997, p. 8311-8317.

Research output: Contribution to journalArticle

Gericke, Arne ; Smith, Elizabeth R. ; Moore, David J. ; Mendelsohn, Richard ; Storch, Judith. / Adipocyte fatty acid-binding protein : Interaction with phospholipid membranes and thermal stability studied by FTIR spectroscopy. In: Biochemistry. 1997 ; Vol. 36, No. 27. pp. 8311-8317.
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