AI Article Synopsis
- L-FABP is a protein in enterocytes that helps solubilize fatty acids and may influence the absorption of fats and drugs.
- This study focuses on how L-FABP interacts with different types of fibrate drugs, including those with carboxylic acid or ester groups.
- Findings indicate that the binding dynamics and energy differ between fibrates with a carboxylate group and those without, shedding light on the mechanisms of molecular recognition by L-FABP.
Article Abstract
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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/jm801349e | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!