Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin

Yoshikawa, H; Hirano, Atsushi; Arakawa, Tsutomu; Shiraki, Kentaro

doi:10.1016/j.ijbiomac.2012.03.014

Cited by 64 publications

(41 citation statements)

References 27 publications

(31 reference statements)

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“…Our findings are consistent with those of Arroyo‐Maya and others () who reported for α‐LA an increase of about 35% β‐strands and a decrease of about 26% in α‐helix content during particulation using 1:4 ratio of acetone. Yoshikawa and others () also showed that in the presence of 0% to 50% ethanol, native Bovine Serum Albumin (BSA) structure changed and it became unfolded. However, the addition of more ethanol 50% to 99% drove BSA molecules to fold again to establish a new structure which was completely different from the initial structure.…”

Section: Resultsmentioning

confidence: 99%

Effects of Desolvating Agent Types, Ratios, and Temperature on Size and Nanostructure of Nanoparticles from α‐Lactalbumin and Ovalbumin

Etorki

Gao

Sadeghi

et al. 2016

Journal of Food Science

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In this study, we compare the preparation of ovalbumin (OVA) and α-lactalbumin (α-LA) nanoparticles using different desolvating agents (ethanol, acetone, and methanol) and water: desolvating agent volume ratios (1:3, 1:4, 1:5, 1:10, and 1:20). Also the effects of protein solution temperature (25, 50, and 80 ℃) on the size of nanoparticles and the stability of crosslinked nanoparticles for 30 d were studied. OVA and α-LA were shown to be good candidates for nanoparticulation and nanoparticles in the range of 60 to 230 nm were obtained. The comparison between the 2 proteins offers guidance to optimize OVA and α-LA nanoparticle fabrication and to efficiently obtain nanoparticles with desired characteristics. The particle sizes of OVA nanoparticles were found to be in the range of 60 to 160 nm, and the particle sizes of α-LA were between 150 and 230 nm. The sizes varied with different desolvating agents: for OVA, ethanol, and methanol both produced nanoparticles smaller than 100 nm; for α-LA, methanol produced the smallest nanoparticles. Water: desolvating agent ratios, in the studied range, did not show a significant effect on the particle sizes for both OVA and α-LA nanoparticles. The size and morphology of the nanoparticles were found to change when the protein solutions were heated up to 50 and 80 ℃ and cooled down before nanoparticulation and most nanoparticles had a smaller diameter.

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Section: Resultsmentioning

confidence: 99%

Effects of Desolvating Agent Types, Ratios, and Temperature on Size and Nanostructure of Nanoparticles from α‐Lactalbumin and Ovalbumin

Etorki

Gao

Sadeghi

et al. 2016

Journal of Food Science

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“…Our results show that the entropy gain in the protein surpasses the unfavorable enthalpy change and drives the nonspecific alcohol binding. In addition, it was suggested that in non-aqueous alcohols or high concentration aqueous alcohol solutions, a large number of alcohol molecules can penetrate into the hydrophobic interior of the protein and extensively break the native protein structure, resulting in dramatic conformational changes and even unfolding of the protein 13, 14, 19, 53, 59, 60 . The denaturation of BSA at higher alcohol pressures (Figure 1 and Supporting Information Figure S1) further proves that those nonspecifically bound alcohols do “mix” with the protein, and if the “mixing” is too extensive, the intramolecular protein interactions are substantially disrupted causing denaturation.…”

Section: Discussionmentioning

confidence: 99%

Dominant Alcohol–Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism

Chong

Kleinhammes

Tang³

et al. 2015

J. Phys. Chem. B

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Water plays an important role in weak associations of small drug molecules with proteins. Intense focus has been on binding-induced structural changes in the water network surrounding protein binding sites, especially their contributions to binding thermodynamics. However, water is also tightly coupled to protein conformations and dynamics, and so far little is known about the influence of water-protein interactions on ligand binding. Alcohols are a type of low-affinity drugs, and it remains unclear how water affects alcohol-protein interactions. Here, we present alcohol adsorption isotherms under controlled protein hydration using in-situ NMR detection. As functions of hydration level, Gibbs free energy, enthalpy, and entropy of binding were determined from the temperature dependence of isotherms. Two types of alcohol binding were found. The dominant type is low-affinity nonspecific binding, which is strongly dependent on temperature and the level of hydration. At low hydration levels, this nonspecific binding only occurs above a threshold of alcohol vapor pressure. An increased hydration level reduces this threshold, with it finally disappearing at a hydration level of h~0.2 (g water/g protein), gradually shifting alcohol binding from an entropy-driven to an enthalpy-driven process. Water at charged and polar groups on the protein surface was found to be particularly important in enabling this binding. Although further increase in hydration has smaller effects on the changes of binding enthalpy and entropy, it results in significant negative change in Gibbs free energy due to unmatched enthalpy-entropy compensation. These results show the crucial role of water-protein interplay in alcohol binding.

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“…[26,27] It has been known for al ongt ime that low concentrations of alcohols stabilize proteins as ar esult of preferentials olvation of the alcohol molecules at the protein surface, [28] and the addition of alcohol induces a-helix formation in ac ertainc lass of proteins, [29][30][31] for which the effect is dependent on the length of the carbon chain of the alcohol. [38][39][40] In ar ecent study, [38] the effect of ethanolo nB SA was found to be bimodal;t he abundance of the secondary structural content was found to be dependent on the concentration of ethanol, which contrasts the findings of other proteins such as lysozyme [34] and melittin. At high alcohol concentrations, the We report the experimentalo bservation of nonmonotonic changes in the collective hydration of bovines erum albumin (BSA) in the presence of alcohols of varying carbon-chain lengths, that is, ethanol, 2-propanol, and tert-butyl alcohol (TBA), by using terahertz (THz) time domain spectroscopy.…”

Section: Introductionmentioning

confidence: 86%

“…This sug- www.chemphyschem.org gests exposure of the hydrophobic moieties of the protein towards the solvent. [38] Upon increasing the concentration, the alcohol molecules actively bind to the protein surface and replace the hydratedw ater molecules;t his subsequently produces as trong perturbation in the protein structure, as the hydrophobic residues becomee xposed to the alcohol molecules. [30] The resultsa re indicative of the specific nature of the protein-alcoholi nteraction; whereas in some cases the alcohol inducesv olumee xclusion to stabilize the helical content, it may also solvate the hydrophobic side chains and destabilizet he helical content.…”

Section: Measurementsmentioning

confidence: 99%

Nonmonotonic Hydration Behavior of Bovine Serum Albumin in Alcohol/Water Binary Mixtures: A Terahertz Spectroscopic Investigation

2017

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We report the experimental observation of nonmonotonic changes in the collective hydration of bovine serum albumin (BSA) in the presence of alcohols of varying carbon-chain lengths, that is, ethanol, 2-propanol, and tert-butyl alcohol (TBA), by using terahertz (THz) time domain spectroscopy. We measured the THz absorption coefficient (α) of the protein solutions, and it was observed that α fluctuated periodically as a function of alcohol concentration at a fixed protein concentration. For a fixed alcohol concentration, an increase in the protein concentration resulted in nonmonotonic changes in α; thus, it first decreased rapidly and then increased, which was followed by a shallow decrease. An alcohol-induced α helix to random coil transition of the protein secondary structure was revealed by circular dichroism spectroscopy measurements, and the effect was most prominent in TBA. The anomalous change in the hydration was found to be a delicate balance between the various interactions present in the three-component system.

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Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin

Cited by 64 publications

References 27 publications

Effects of Desolvating Agent Types, Ratios, and Temperature on Size and Nanostructure of Nanoparticles from α‐Lactalbumin and Ovalbumin

Effects of Desolvating Agent Types, Ratios, and Temperature on Size and Nanostructure of Nanoparticles from α‐Lactalbumin and Ovalbumin

Dominant Alcohol–Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism

Nonmonotonic Hydration Behavior of Bovine Serum Albumin in Alcohol/Water Binary Mixtures: A Terahertz Spectroscopic Investigation

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