期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 52, 期 17, 页码 5344-5355出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm801349e
关键词
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资金
- Australian Postgraduate Scholarship
- National Health and Medical Research Council, Australia [384300]
- Australian Research Council [DP0342458, DP0664069]
- Australian Research Council [DP0342458, DP0664069] Funding Source: Australian Research Council
Liver-fatty acid binding protein (L-FABP) is found in high levels in enterocytes and is involved in cytosolic solubilization of fatty acids. In addition, L-FABP has been shown to bind endogenous and exogenous lipophilic compounds, suggesting that it may also play a role in modulating their absorption and disposition within enterocytes. Previously, we have described binding of L-FABP to a range of drugs, including a series of fibrates. In the present study, we have generated structural models of L-FABP-fibrate complexes and undertaken thermodynamic analysis of the binding of fibrates containing either a carboxylic acid or ester functionality. Analysis of the current data reveals that both the location and the energetics of binding are different for fibrates that contain a carboxylate compared to those that do not. As such, the data presented in this study suggest potential mechanisms that underpin molecular recognition and dictate specificity in the interaction between fibrates and L-FABP.
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