ArticleBiochemistry and biophysics reports2017
Protocols and pitfalls in obtaining fatty acid-binding proteins for biophysical studies of ligand-protein and protein-protein interactions.
Article in Biochemistry and biophysics reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- A high-resolution data set of fatty acid-binding protein structures. I. Dynamics of FABP4 and ligand binding.Acta crystallographica. Section D, Structural biology · 2025Article
- Broad PFAS Binding with Fatty Acid Binding Protein 4 Is Enabled by Variable Binding Modes.JACS Au · 2025Article
- Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein 1 (FABP1) and FABP1 Binding Alters Drug Metabolism.Molecular pharmacology · 2024Article
- Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein (FABP1) and FABP1 Binding Alters Drug Metabolism.bioRxiv : the preprint server for biology · 2024Article
- Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein.Science (New York, N.Y.) · 2020Article
- Two fatty acid-binding proteins expressed in the intestine interact differently with endocannabinoids.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Adipocyte fatty acid-binding protein (AFABP: FABP4) is a member of the intracellular lipid-binding protein family that is thought to target long-chain fatty acids to nuclear receptors such as peroxisome proliferator-activated receptor gamma (PPARγ), which in turn plays roles in insulin resistance and obesity. A molecular understanding of AFABP function requires robust isolation of the protein in liganded and free forms as well as characterization of its oligomerization state(s) under physiological conditions. We report development of a protocol to optimize the production of members of this protein family in pure form, including removal of their bound lipids by mixing with hydrophobically functionalized hydroxypropyl dextran beads and validation by two-dimensional NMR spectroscopy. The formation of self-associated or covalently bonded protein dimers was evaluated critically using gel filtration chromatography, revealing conditions that promote or prevent formation of disulfide-linked homodimers. The resulting scheme provides a solid foundation for future investigations of AFABP interactions with key ligand and protein partners involved in lipid metabolism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.