Denaturation and aggregation of lysozyme in water-ethanol solution.

Szymańska, Agnieszka; Hornowski, T.; Ślósarek, G.

doi:10.18388/abp.2012_2158

Cited by 13 publications

(7 citation statements)

References 34 publications

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“…These aggregates were progressively disrupted during shearing, resulting in a lower solution viscosity [36,38]. Newtonian behavior of low concentration BSA, LYS and OVL solutions is in agreement with previous studies [39][40][41]. The decrease of ALG + calcium shear stress within 0.1 -3 s -1 shear rate range was due to the rupture of the egg-box polymer network.…”

Section: Characterization Of Foulantssupporting

confidence: 86%

Impact of intrinsic properties of foulants on membrane performance in osmotic desalination applications

Arkhangelsky

Lay

Wicaksana

et al. 2014

Separation and Purification Technology

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Section: Characterization Of Foulantssupporting

confidence: 86%

Impact of intrinsic properties of foulants on membrane performance in osmotic desalination applications

Arkhangelsky

Lay

Wicaksana

et al. 2014

Separation and Purification Technology

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“…Biswas and co-workers have assigned such anomalies to a structural transition at those concentrations; however, the particular nature of the aforementioned structural transition was left unresolved. On the other hand, many computational − and experimental − studies have been performed regarding the impacts of aqueous binary mixtures on the structures of proteins, polymers, and several other systems. By using fluorescence correlation spectroscopy and molecular dynamics simulation, Bhattacharyya and co-workers , have manifested that the structure and function of a protein can be altered to a significant extent by regulating the concentration of ethanol in water–ethanol binary mixtures.…”

Section: Introductionmentioning

confidence: 99%

Unravelling the Composition-Dependent Anomalies of Pair Hydrophobicity in Water–Ethanol Binary Mixtures

Halder

Jana

2018

J. Phys. Chem. B

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Aqueous binary mixtures have received immense attention in recent years because of their extensive application in several biological and industrial processes. The water-ethanol binary mixture serves as a unique system because it exhibits composition-dependent alteration of dynamic and thermodynamic properties. Our present work demonstrates how different compositions of water-ethanol binary mixtures affect the pair hydrophobicity of different hydrophobes. Pair hydrophobicity is measured by the depth of the first minimum (contact minima) of potential of mean force (PMF) profile between two hydrophobes. The pair hydrophobicity is found to be increased with addition of ethanol to water up to a mole fraction of x = 0.10 and decreased with further addition of ethanol. This observation is shown to be true for three (methane-methane, isobutane-isobutane, and toluene-toluene) different pairs of hydrophobes. Decomposition of PMF into enthalpic and entropic contribution indicates a switch from entropic to enthalpic stabilization of the contact minimum upon addition of ethanol to water. The gain in mixing enthalpy of the binary solvent system upon association of two hydrophobes is found to be the determining factor for the stabilization of contact minimum. Several static/dynamics quantities (average composition fluctuations, diffusion coefficients, fluctuations in total dipole moment, propensity of ethyl-ethyl association, etc) of the ethanol-water binary mixture also show irregularities around x = 0.10-0.15. We have also discovered that the hydrogen bonding pattern of ethanol rather than water reveals a change in trend near the similar composition range. As the anomalous behavior of the physical/dynamical properties along with the pair hydrophobicity in an aqueous binary mixture of amphiphilic solutes is a common phenomenon, our results may provide a general viewpoint on these aspects.

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“…Ethanol is reported to induce protein aggregation with increase in concentration in experimental results. 36 …”

Section: Introductionmentioning

confidence: 99%

Effect of Urea, Arginine, and Ethanol Concentration on Aggregation of ₁₇₉CVNITV₁₈₄ Fragment of Sheep Prion Protein

Jahan

Nayeem

2018

ACS Omega

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Understanding protein aggregation is of utmost importance as it is responsible for causing several neurodegenerative diseases and one of the serious impediments in large-scale biopharmaceutical production. The prion protein is responsible for pathological states in fatal transmissible spongiform conditions, such as Creutzfeldt–Jakob disease and bovine spongiform encephalopathy. The peptide fragment 178–191 of Syrian hamster prion protein is known to be amyloidogenic. Here, we identified the fragment 179CVNITV184 as an aggregation-prone fragment in sheep prion protein. This fragment is conserved sequence among sheep and Syrian hamster prion protein and also falls in the previously identified amyloidogenic sequence. The mechanistic details of the aggregation behavior are analyzed in three different concentrations of urea, arginine, and ethanol. Urea and arginine are found to be aggregation suppressors, but ethanol enhances the protein aggregation through β-sheet formation. We have also analyzed the influence of these osmolyte on water dynamics in the presence of the octamer of this aggregation-prone fragment and correlated this water dynamics with the aggregation behavior of the octamer.

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Denaturation and aggregation of lysozyme in water-ethanol solution.

Cited by 13 publications

References 34 publications

Impact of intrinsic properties of foulants on membrane performance in osmotic desalination applications

Impact of intrinsic properties of foulants on membrane performance in osmotic desalination applications

Unravelling the Composition-Dependent Anomalies of Pair Hydrophobicity in Water–Ethanol Binary Mixtures

Effect of Urea, Arginine, and Ethanol Concentration on Aggregation of ₁₇₉CVNITV₁₈₄ Fragment of Sheep Prion Protein

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Denaturation and aggregation of lysozyme in water-ethanol solution.

Cited by 13 publications

References 34 publications

Impact of intrinsic properties of foulants on membrane performance in osmotic desalination applications

Impact of intrinsic properties of foulants on membrane performance in osmotic desalination applications

Unravelling the Composition-Dependent Anomalies of Pair Hydrophobicity in Water–Ethanol Binary Mixtures

Effect of Urea, Arginine, and Ethanol Concentration on Aggregation of 179CVNITV184 Fragment of Sheep Prion Protein

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Effect of Urea, Arginine, and Ethanol Concentration on Aggregation of ₁₇₉CVNITV₁₈₄ Fragment of Sheep Prion Protein