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Characterization of lipophilic drug binding to rat intestinal fatty acid binding protein

journal contribution
posted on 2009-06-01, 00:00 authored by Tony Velkov, M Lim, J Horne, J Simpson, Christine Porter, M Scanlon
Intestinal fatty acid binding protein (I-FABP) is present at high levels in the absorptive cells of the intestine (enterocytes) where it plays a role in the intracellular solubilization of fatty acids (FA). However, I-FABP has also been shown to bind to a range of non-FA ligands, including some lipophilic drug molecules, albeit with generally lower affinity than FA. The significance of these lower affinity interactions with exogenous compounds is not known. In this manuscript, we describe further characterization of drug-rat I-FABP binding interactions using a thermal-shift assay. A structural explanation of the observed affinity of rat I-FABP for different drugs based on spectroscopic data and modeling experiments is presented. In addition, immunocytochemistry has been used to probe the expression of I-FABP in a cell culture model reflective of the absorptive cells of the small intestine. Taken together, these data suggest a possible role for I-FABP in the disposition of some lipophilic drugs within the enterocyte.

History

Journal

Molecular and cellular biochemistry

Volume

326

Issue

1-2

Pagination

87 - 95

Publisher

Kluwer Academic Publishers

Location

New York, N.Y.

ISSN

0300-8177

eISSN

1573-4919

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2009, Springer Science+Business Media, LLC

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