Fibrillation of hen egg white lysozyme triggers reduction of copper(II)

Ghosh, Sudeshna; Pandey, Nitin; Bhattacharya, Susmita; Roy, Anushree; Dasgupta, Swagata

doi:10.1016/j.ijbiomac.2012.04.024

Cited by 30 publications

(10 citation statements)

References 47 publications

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“…2a), the carbon and oxygen peaks were observed on the XPS scans. After the (LY-HTCC/ALG) 10.5 film deposition, the presence of sulfur, carbon, nitrogen, and oxygen on the surface of composite mats was attributed to proteinaceous nature of the mineralized substrate, lysozyme is a globular protein with 129 amino acid residues that comprise two different domains cross-linked by means of four disulfide bonds [26], the sequence of LY in particular contains 12 sulfur bearing cysteine and methionine residues [27]. A new sulfur peak (S 2p) around 165 eV was found in the XPS spectrum (Fig.…”

Section: Morphology Of the Fibrous Matsmentioning

confidence: 99%

Antibacterial multilayer films fabricated by LBL immobilizing lysozyme and HTCC on nanofibrous mats

Huang

Xue

et al. 2013

International Journal of Biological Macromolecules

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Section: Morphology Of the Fibrous Matsmentioning

confidence: 99%

Antibacterial multilayer films fabricated by LBL immobilizing lysozyme and HTCC on nanofibrous mats

Huang

Xue

et al. 2013

International Journal of Biological Macromolecules

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“…The ratios of β-sheet:α-helical components are very close to the values for these fibrils reported from CD measurements. 36,37 Hence, the distributions of ψ angles related to αhelix and β-sheet are obtained. In Figure 5, the solid line describes the distribution of ψ angle in HSA and HEWL native proteins (as obtained earlier), while the dotted line describes the same for their fibrillar state.…”

Section: Resultsmentioning

confidence: 99%

“…The solutions were then centrifuged at 6000 rpm for 30 min to separate the fibrils. The detail protocols of preparing HSA and HEWL fibrils are available in refs and . More details on HGC c isolation will be reported elsewhere.…”

Section: Materials and Methodsmentioning

confidence: 99%

Distribution of Protein Ramachandran Psi (ψ) Angle Using Non-Resonance Visible Raman Scattering Measurements

et al. 2013

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Knowing the distribution of Ramachandran angles helps in understanding peptide and protein backbone conformation. Empirical relations are proposed to correlate the spectral profile of the amide III3 band, obtained from ultraviolet resonance Raman measurements (UVRR), with the Ramachandran dihedral psi angle distribution in small peptide and protein molecules, in different environmental conditions (Mikhonin et al. J. Phys. Chem. B 2006, 110, 1928-1943). It has also been used for more complicated structures, like large globular proteins and protein fibrils. In our work here, we use visible Raman spectra and available empirical relations to obtain similar correlations for human serum albumin, hen egg white lysozyme, and human gamma crystallin. We also report the dihedral angle distribution in fibrils and a denatured protein in an ethanol environment using the same spectroscopic technique.

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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%

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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Fibrillation of hen egg white lysozyme triggers reduction of copper(II)

Cited by 30 publications

References 47 publications

Antibacterial multilayer films fabricated by LBL immobilizing lysozyme and HTCC on nanofibrous mats

Antibacterial multilayer films fabricated by LBL immobilizing lysozyme and HTCC on nanofibrous mats

Distribution of Protein Ramachandran Psi (ψ) Angle Using Non-Resonance Visible Raman Scattering Measurements

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

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