Binding properties of Echinococcus granulosus fatty acid binding protein

Citation
G. Alvite et al., Binding properties of Echinococcus granulosus fatty acid binding protein, BBA-MOL C B, 1533(3), 2001, pp. 293-302
Citations number
50
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
ISSN journal
13881981 → ACNP
Volume
1533
Issue
3
Year of publication
2001
Pages
293 - 302
Database
ISI
SICI code
1388-1981(20011031)1533:3<293:BPOEGF>2.0.ZU;2-2
Abstract
EgFABP1 is a developmentally regulated intracellular fatty acid binding pro tein characterized in the larval stage of parasitic platyhelminth Echinococ cus granulosus. It is structurally related to the heart group of fatty acid binding proteins (H-FABPs). Binding properties and ligand affinity of reco mbinant EgFABP1 were determined by fluorescence spectroscopy using cis- and trans-parinaric acid. Two binding sites for cis- and trans-parinaric acid were found (K-d(1) 24 +/- 4 nM, K-d(2) 510 +/- 60 nM for cis-parinaric acid and K-d(1) 32 +/- 4 nM, K-d(2) 364 +/- 75 nM for trans-parinaric). A putat ive third site for both fatty acids is discussed. Binding preferences were determined using displacement assays. Arachidonic and oleic acids presented the highest displacement percentages for EgFABP1. The Echinococcus FABP is the unique member of the H-FABP group able to bind two long chain fatty ac id molecules with high affinity. Structure-function relationships and putat ive roles for EgFABP1 in E. granulosus metabolism are discussed. (C) 2001 E lsevier Science B.V. All rights reserved.