Monoglyceride-Protein Interaction. The Binding of Monoolein to Native Human Serum Albumin.

Arvidsson, E. O.; Belfrage, Per; Hultin, Eskil; Liljeqvist, Gisela; Lindberg, Alf A.; Jansen, Gert; Lamm, Bo; Samuelsson, Benny

doi:10.3891/acta.chem.scand.23-0232

Cited by 27 publications

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“…We first measured the binding affinities of CA, MC, and ME to solution-phase BSA proteins by steady-state fluorescence spectroscopy (Figure and Table S1). Like how fatty acids can insert into hydrophobic pockets on the BSA protein surface, it is known that monoglycerides − and fatty acid methyl esters , can bind similarly to serum albumin proteins in some cases. We evaluated the fluorescence emission spectra corresponding to the intrinsic fluorescence of tryptophan residues in BSA alone and in BSA together with varying amounts of CA, MC, or ME (Figure A–C).…”

Section: Resultsmentioning

confidence: 99%

Elucidating How Different Amphipathic Stabilizers Affect BSA Protein Conformational Properties and Adsorption Behavior

et al. 2020

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Natural proteins such as bovine serum albumin (BSA) are readily extracted from biological fluids and widely used in various applications such as drug delivery and surface coatings. It is standard practice to dope BSA proteins with an amphipathic stabilizer, most commonly fatty acids, during purification steps to maintain BSA conformational properties. There have been extensive studies investigating how fatty acids and related amphiphiles affect solution-phase BSA conformational properties, while it is far less understood how amphipathic stabilizers might influence noncovalent BSA adsorption onto solid supports, which is practically relevant to form surface coatings. Herein, we systematically investigated the binding interactions between BSA proteins and different molar ratios of caprylic acid (CA), monocaprylin (MC), and methyl caprylate (ME) amphiphilesall of which have 8-carbon-long, saturated hydrocarbon chains with distinct headgroupsand resulting effects on BSA adsorption behavior on silica surfaces. Our findings revealed that anionic CA had the greatest binding affinity to BSA, which translated into greater solution-phase conformational stability and reduced adsorption-related conformational changes along with relatively low packing densities in fabricated BSA adlayers. On the other hand, nonionic MC had moderate binding affinity to BSA and could stabilize BSA conformational properties in the solution and adsorbed states while also enabling BSA adlayers to form with higher packing densities. We discuss physicochemical factors that contribute to these performance differences, and our findings demonstrate how rational selection of amphiphile type and amount can enable control over BSA adlayer properties, which could lead to improved BSA protein-based surface coatings.

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Section: Resultsmentioning

confidence: 99%

Elucidating How Different Amphipathic Stabilizers Affect BSA Protein Conformational Properties and Adsorption Behavior

et al. 2020

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“…Albumin is the major serum transport protein and the ligand binding properties of this protein have been studied in great detail, especially with regard to drugs and longchain fatty acids (1,2). The products of triglyceride metabolism by lipases are fatty acids, which bind to HSA at multiple sites with varying affinities (1-3), and 2-monoacylglycerides, for which there is minimal binding information (5). The multiple binding sites on albumin and the non-polar natures of the ligands make it difficult to perform definitive binding studies.…”

Section: Discussionmentioning

confidence: 99%

Monoacylglycerol binding to human serum albumin: Evidence that monooleoylglycerol binds at the dansylsarcosine site

Thumser

Buckland

Wilton

1998

Journal of Lipid Research

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The binding of monoacylglycerides of long-chain fatty acids to human serum albumin has been examined using monooleoylglycerol as the ligand. Binding was investigated using changes in tryptophan fluorescence and also the displacement of a variety of well-studied fluorescent ligands from human serum albumin (HSA). Monooleoylglycerol caused a decrease in fluorescence from tryptophan-214 when measured at 350 nm while oleic acid had no effect on fluorescence at this wavelength and did not compete with monooleoylglycerol. In contrast, oleic acid caused an increase in fluorescence at 330 nm whereas monooleoylglycerol did not affect fluorescence intensity at this wavelength. These results suggest that these two ligands do not bind to the same site on HSA. From competition studies using dansylglycine, dansylsarcosine, 11-(dansylamino)-undecanoic acid and 1-anilino-8-naphthalenesulfonic acid it was proposed that monooleoylglycerol binds at the dansylsarcosine site (site II) of HSA. Monooleoylglycerol was a competitive inhibitor of dansylsarcosine binding with a K d of about 2.5 M whereas oleic acid was not competitive with dansylsarcosine binding.-Thumser, A. E. A., A. G. Buckland, and D. C. Wilton. Monoacylglycerol binding to human serum albumin: evidence that monooleoylglycerol binds at the dansylsarcosine site.

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“…Triacylglycerol (TG) in chylomicra is hydrolyzed by LPL, which cleaves the ester bonds at the 1-and 3-TG positions, producing free fatty acids (FFA) and 2-MG. Several theories are currently proposed for the metabolic fate of 2-MG post-TG hydrolysis, including the following: 2-MG diffuse away from the site of lipolysis and fuse with cell membranes (9,10), 2-MG are bound and transported by serum albumin (11,12), 2-MG remain in chylomicra remnants or transfer to low density lipoprotein and high density lipoprotein, which are then taken up by the liver (13,14), and 2-MG spontaneously isomerize to 1(3)-MG, which are then hydrolyzed by LPL to glycerol and FFA (1)(2)(3)15). None of these theories, however, is supported by a consensus of scientific evidence.…”

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confidence: 99%

Kinetics of 2‐monoacylglycerol acyl migration in model chylomicra

Lyubachevskaya

Boyle-Roden

2000

Lipids

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In the metabolism of triacylglycerol (TG)-rich lipoproteins, 2-monoacylglycerols (2-MG) are produced by lipoprotein lipase (LPL) hydrolysis of TG. The metabolic fate of 2-MG is not known with certainty. 2-MG that accumulate on the chylomicra surface have been proposed to isomerize spontaneously to 1(3)-MG, which are then hydrolyzed by LPL to free fatty acids and glycerol. In this study the rate and the effect of acyl chain saturation on the spontaneous acyl migration of 2-MG in in vitro model chylomicra emulsions were determined. After 1 h of incubation at 37 degrees C, less than 20% of 2-monoolein (2-MO) or 2-monopalmitin (2-MP) spontaneously isomerized to 1(3)-MO or 1(3)-MP, respectively. Accordingly, it was concluded that spontaneous isomerization of 2-MG is not the major mechanism for 2-MG metabolism post-TG hydrolysis in chylomicra. Isomerization rates, expressed as decrease in percentage of 2-MG remaining per hour, were -5.12 and -5.86 in water, and -0.43 and -0.41 in hexane for 2-MO and 2-MP, respectively. There was no significant difference between the isomerization rates of 2-MO and 2-MP. Thus, in the present study, saturation of the MG acyl chain did not influence spontaneous acyl migration in either water or hexane, but isomerization of 2-MG was faster in water than in hexane.

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Monoglyceride-Protein Interaction. The Binding of Monoolein to Native Human Serum Albumin.

Cited by 27 publications

References 0 publications

Elucidating How Different Amphipathic Stabilizers Affect BSA Protein Conformational Properties and Adsorption Behavior

Elucidating How Different Amphipathic Stabilizers Affect BSA Protein Conformational Properties and Adsorption Behavior

Monoacylglycerol binding to human serum albumin: Evidence that monooleoylglycerol binds at the dansylsarcosine site

Kinetics of 2‐monoacylglycerol acyl migration in model chylomicra

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