Encapsulating biological materials in lipid vesicles is of interest for mimicking cells; however, except in some particular cases, such processes do not occur spontaneously. Herein, we developed a simple and robust method for encapsulating proteins in fatty acid vesicles in high yields. Fatty acid based, membrane-free coacervates spontaneously sequester proteins and can reversibly form membranous vesicles upon varying the pH value, the precrowding feature in coacervates allowing for protein encapsulation within vesicles. We then produced enzyme-enriched vesicles and show that enzymatic reactions can occur in these micrometric capsules. This work could be of interest in the field of synthetic biology for building microreactors.Vesicular microreactors: Fatty acid based, membrane-free coacervates spontaneously sequester proteins and can reversibly form membranous vesicles upon changing the pH value, which leads to protein encapsulation within the vesicles. These micrometric capsules also provide a suitable environment for enzymatic reactions.
Branched Fatty Acid Esters of Hydroxy Fatty AcidsAre Preferred Substrates of the MODY8 Protein Carboxyl Ester Lipase
Branched Fatty Acid Esters of Hydroxy Fatty AcidsAre Preferred Substrates of the MODY8 Protein Carboxyl Ester Lipase
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00565/20160810/images/medium/bi-2016-005654_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00565
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An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
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Authors: He Y, Estephan R, Yang X, Vela A, Wang H, Bernard C, Stark RE
Liver fatty acid-binding protein (LFABP) is a 14-kDa cytosolic polypeptide, differing from other family members in number of ligand binding sites, diversity of bound ligands, and transfer of fatty acid(s) to...
nmrlearner
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01-14-2011 12:05 PM
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Biochemistry. 2005 Feb 22;44(7):2369-77
Authors: Li H, Frieden C
(19)F-Nuclear magnetic resonance (NMR) studies have been carried out after incorporation of 4-(19)F-phenylalanine into the intestinal fatty acid binding protein (IFABP), a...
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Biochem Biophys Res Commun. 2004 Oct 22;323(3):987-95
Authors: Osiro D, Muniz JR, Coleta Filho HD, de Sousa AA, Machado MA, Garratt RC, Colnago LA
Xylella fastidiosa was the first plant pathogen to have its complete genome sequence elucidated. Routine database analyses suggested that two enzymes...
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The interactions of fatty acids with proteins have been studied by a variety of conventional approaches for decades. However, only limited aspects of fatty acid-protein interactions have been elucidated, even with the integration of information gleaned from the many techniques....
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[NMR paper] Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C
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Biochemistry. 2001 Oct 23;40(42):12604-11
Authors: Beringhelli T, Goldoni L, Capaldi S, Bossi A, Perduca M, Monaco HL
Two different groups of liver fatty acid-binding proteins (L-FABPs) are known: the mammalian type and the basic type. Very few members of this second group of L-FABPs have been...
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Mol Cell Biochem. 1990 Oct 15-Nov 8;98(1-2):101-10
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A high-resolution, solution-state NMR method for characterizing and comparing the interactions between carboxyl 13C-enriched fatty acids (FA) and...
Sequestration of Proteins by Fatty Acid Coacervates for Their Encapsulation within Vesicles
Linear Mode
