Denaturation and aggregation of hen egg lysozyme in aqueous ethanol solution studied by dynamic light scattering

Tanaka, Shinpei; Oda, Yutaka; Ataka, Mitsuo; Onuma, Kazuo; Fujiwara, Satoru; Yonezawa, Yasushige

doi:10.1002/1097-0282(20011015)59:5<370::aid-bip1034>3.0.co;2-z

Cited by 51 publications

(10 citation statements)

References 18 publications

(46 reference statements)

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“…The amyloid structure formation has been studied by several experimental techniques -radiation scattering measurements [12][13][14][15][16], circular dichroism [17] and X-ray diffraction [18]. In this paper we present studies of the aggregation and denaturation processes of hen egg white lysozyme (HEWL) initiated by the presence of ethanol molecules using the methods of small angle X-ray scattering (SAXS) and rheological experiments.…”

Section: Introductionsupporting

confidence: 76%

The SAXS and Rheological Studies of HEWL Amyloid Formation

et al. 2008

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We performed small angle X-ray scattering and rheological experiments in order to analyze the aggregation and denaturation processes of hen egg white lysozyme initiated by the presence of ethanol molecule. At low ethanol concentrations (below 60% (v/v)) we did not observe any change of the radius of gyration of lysozyme and no drastic changes in viscosity of the protein solution. With the increase in ethanol concentration up to the final concentration of 85% (v/v) the viscosity of protein solution dramatically increased. For high ethanol concentration a pseudoplastic behavior of lysozyme solution was observed, indicating a process of aggregation and reorientation of the protein molecules. Similar effects were observed in small angle X-ray scattering experiments. We assume that the analysis of the aggregation processes of the hen egg white lysozyme could contribute to our understanding of the mechanism of lysozyme amyloid formation.

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Section: Introductionsupporting

confidence: 76%

The SAXS and Rheological Studies of HEWL Amyloid Formation

et al. 2008

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“…With the increasing amount of ethanol D T decreases (Fig. 2) as it was also observed earlier [20,21]. The diusion coecient reaches a value of (0.689±0.011)×10…”

Section: Resultsmentioning

confidence: 99%

Light Scattering Studies of Hydration and Structural Transformations of Lysozyme

Szymańska

Ślósarek

2012

Acta Phys. Pol. A

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We have applied the method of dynamic light scattering to analyse the lysozymeethanol interaction. For low ethanol concentration (below 4.3% (v/v)) no chemical denaturation process is observed. When the ethanol concentration grows above the triggering concentration the hydrodynamic radius of lysozyme increases, indicating the structural changes within the protein molecule. The observed structural modications are attributed to dehydration and preliminary tertiary structure modication of the protein molecule.

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“…Hen egg-white lysozyme (HEWL) forms amyloid fibrils at high concentrations in aqueous solutions under a variety of pH conditions [2], ionic strengths [3,4], and temperatures [2,5,6], or in organic solvents such as alcohols [7][8][9][10][11][12]. HEWL has been studied extensively and is closely related to human lysozyme, variants of which form amyloid fibrils that are related to hereditary systemic amyloidosis.…”

Section: Introductionmentioning

confidence: 99%

“…Far-UV circular dichroism (CD) revealed a change in the secondary structure of lysozyme molecules in the higher temperature range with increasing pH [5]. In another approach, amyloid fibrils formed with increasing ethanol concentration [8][9][10]. Yonezawa et al investigated the structures of HEWL in various concentrations of ethanol, and proposed that the following structural states: the monomer state; the dimer-formation state; the protofilament-formation state; the protofilament state; and the ultimate formation of amyloid fibrils, which occurred at an ethanol concentration of 90% vol [10].…”

Section: Introductionmentioning

confidence: 99%

“…They suggested that the gels are formed by the connection between molecules by the intermolecular β-sheet formation with the apparent peak at 4.7 Å in x-ray diffraction experiment. It is the same as the distance between peptide chains in the β-sheet structure [8]. To clarify the gelling process in more details, we have interpreted the gelation mechanism with DLS technique.…”

Section: Introductionmentioning

confidence: 99%

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Dynamics of amyloid-like aggregation and gel formation of hen egg-white lysozyme in highly concentrated ethanol solution

et al. 2017

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We investigated the mechanisms of amyloidlike aggregation and gel formation in hen egg-white lysozyme (HEWL) in a mixed solvent comprising 90% v/v ethanol in water using dynamic light scattering (DLS) and circular dichroism CD. The mechanism of HEWL in ethanol aqueous solution is interpreted into three stages as: (I) denaturation of HEWL; (II) elongation of amyloid fibrils composed of β-sheet-rich HEWL by lateral aggregation; and (III) gel formation due to the creation of junctions in amyloid fibrils. The transformation of sol to gel can be confirmed by: (1) the oscillation behavior and the rapid increase in the intensity of scattered light; (2) the power-law behavior of the correlation function of scattered light g (2) (t); (3) the appearance of a long-time tail in the distribution function of the decay time G(τ); and (4) the beginning of the reduction in initial amplitude in g (2) (t). The gelation rate was strongly dependent on the protein concentration. The estimated rod length of the amyloid fibrils increased significantly over time. Scanning electron microscopy (SEM) performed on the formation of fibrils in the HEWL gels revealed that the structure was highly heterogeneous, with areas characterized by dense fiber networks interspersed with loose network areas.

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Denaturation and aggregation of hen egg lysozyme in aqueous ethanol solution studied by dynamic light scattering

Cited by 51 publications

References 18 publications

The SAXS and Rheological Studies of HEWL Amyloid Formation

The SAXS and Rheological Studies of HEWL Amyloid Formation

Light Scattering Studies of Hydration and Structural Transformations of Lysozyme

Dynamics of amyloid-like aggregation and gel formation of hen egg-white lysozyme in highly concentrated ethanol solution

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