The integrity of the α-helical domain of intestinal fatty acid binding protein is essential for the collision-mediated transfer of fatty acids to phospholipid membranes
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TLDR
The results indicate that the alphaI-helix is crucial for IFABP collisional FA transfer, and further indicate the participation of the alphaII-helIX in the formation of a protein-membrane "collisional complex".About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2008-04-01 and is currently open access. It has received 22 citations till now. The article focuses on the topics: Fatty acid-binding protein.read more
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Journal ArticleDOI
Enterocyte fatty acid-binding proteins (FABPs): Different functions of liver and intestinal FABPs in the intestine
Angela M. Gajda,Judith Storch +1 more
TL;DR: The evolving knowledge of the functions of LFABP and IFABP in the intestinal enterocyte is discussed, indicating that these proteins indeed have different functions in intestinal lipid metabolism and whole body energy homeostasis.
Journal ArticleDOI
Fatty Acid-Binding Protein 5 Facilitates the Blood-Brain Barrier Transport of Docosahexaenoic Acid.
Yijun Pan,Martin J. Scanlon,Yuji Owada,Yui Yamamoto,Christopher J.H. Porter,Joseph A. Nicolazzo +5 more
TL;DR: It is demonstrated that FABP5 binds to DHA and is involved in the brain endothelial cell uptake and subsequent BBB transport of DHA, confirming the importance of this cytoplasmic carrier protein in the CNS exposure of this PUFA essential for neuronal function.
Journal ArticleDOI
NMR investigation of the equilibrium partitioning of a water-soluble bile salt protein carrier to phospholipid vesicles
Alberto Ceccon,Mariapina D'Onofrio,Serena Zanzoni,Dario Livio Longo,Silvio Aime,Henriette Molinari,Michael Assfalg +6 more
TL;DR: The BABP‐liposome interaction was investigated for the first time through an MRI‐chemical exchange saturation transfer experiment that has potential applications not only in the field of biology, but also in biomedicine, bioanalytical chemistry, and nanotechnology.
Journal ArticleDOI
Interaction of enterocyte FABPs with phospholipid membranes: clues for specific physiological roles.
Lisandro J. Falomir-Lockhart,Gisela Raquel Franchini,Gisela Raquel Franchini,María Ximena Guerbi,Judith Storch,Betina Córsico,Betina Córsico +6 more
TL;DR: It is demonstrated here that, besides their apparently opposite ligand transfer mechanisms, both LFABP and IFABP are able to interact with phospholipid membranes, but the factors that modulate such interactions are different for each protein, further implying different roles for IFABp and LFABp in the intracellular context.
Journal ArticleDOI
The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins
Laura Ragona,Katiuscia Pagano,Simona Tomaselli,Filippo Favretto,Alberto Ceccon,Serena Zanzoni,Mariapina D'Onofrio,Michael Assfalg,Henriette Molinari +8 more
TL;DR: This review is intended to summarize and possibly generalize the results up to now described, providing a picture which could help to identify the missing notions necessary to improve the understanding of the role of dynamics in iLBPs' molecular recognition.
References
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Journal ArticleDOI
A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions
TL;DR: These procedures, which can circumvent the need for large-scale phage or plasmid growths, preparative gel-electrophoresis and the screening of molecular clones, can facilitate the rapid study of sequence-specific interactions of proteins and DNA.
Journal ArticleDOI
Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
TL;DR: It has been shown that fast protein size-exclusion liquid chromatography (FPLC) is an "inert" technique that does not shift the equilibrium between N, MG, and U states and, therefore, can be used for qualitative and quantitative studies of protein denaturation.
Book ChapterDOI
The cellular fatty acid binding proteins: aspects of structure, regulation, and function.
TL;DR: This chapter provides a comprehensive overview of the current state of knowledge of the research with particular emphasis on evolving concepts of fatty acid binding proteins (FABP) structure, regulation, and function.
Journal ArticleDOI
The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates.
TL;DR: The crystal structure of the recombinant form of rat liver fatty acid-binding protein was completed to 2.3 Å and refined to an R factor of 19.0%.
Journal ArticleDOI
Expression of rat intestinal fatty acid-binding protein in Escherichia coli. Purification and comparison of ligand binding characteristics with that of Escherichia coli-derived rat liver fatty acid-binding protein.
TL;DR: In this article, the ability of I- and L-FABP to bind fatty acids of different chain length and degree of saturation using a hydroxyalkoxypropyl dextran-based assay was analyzed.
Related Papers (5)
Fatty Acid Transfer from Liver and Intestinal Fatty Acid-binding Proteins to Membranes Occurs by Different Mechanisms
Kuo-Tung Hsu,Judith Storch +1 more
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