An In Vitro elucidation of the antiaggregatory potential of Diosminover thermally induced unfolding of hen egg white lysozyme; A preventive quest for lysozyme amyloidosis

2019 ◽  
Vol 129 ◽  
pp. 1015-1023 ◽  
Author(s):  
Mohammad Furkan ◽  
Mohammad Khursheed Siddiqi ◽  
Syed Mohammad Zakariya ◽  
Faez Iqbal Khan ◽  
Md. Imtaiyaz Hassan ◽  
...  
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Thermally Induced ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

scholarly journals In Vitro, D-Ribose and Formaldehyde Glycating Effects on Hen Egg White Lysozyme

2021 ◽  
Keyword(s):  
Cell Damage ◽  
Egg White ◽  
Cross Linking ◽  
Hen Egg White Lysozyme ◽  
Time Duration ◽  
Experimental Conditions ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Background: Glycation causes severe damage to the protein structure, instigating different diseases like cataracts, nephropathy, vasculopathy, retinopathy, atherosclerosis, neurodegenerative disease, diabetes, and age-dependent complications. Formaldehyde, a pollutant present in human habitation, is produced endogenously or exogenously during cooking or incinerating wood, paints, furniture, chipboards, fabric etc. Its higher concentrations can cause cell damage that promotes the formation of DNA/Protein cross-links. The present study aimed to evaluate the glycating effects of formaldehyde on hen egg white lysozyme in comparison with known glycating agent D-ribose. Methods: In this, in-vitro study, hen egg white lysozyme (HEWL) glycation with different concentrations of formaldehyde (0.25mM, 0.5mM, 1mM and 2mM) and D-ribose (0.01mM, 0.05mM, 0.1mM and 0.5mM) was examined using two different experimental conditions: concentration and time duration. Further cross-linking of protein was also analysed using SDS-PAGE technique. Results: Glycation of HEWL treated with formaldehyde increased with increasing concentrations (0.25mM, 0.5mM, 1mM and 2mM) and time duration (1, 3, 7 and 15 days). Cross linking of HEWL showed visible glycation at 2mM concentration. Cross-linked HEWL products gave dimer at 0.25mM and 0.5mM and trimers at 1mM and 2mMat 3, 7 and 15days. However, compared to formaldehyde, D-ribose glycation at different concentrations (0.01mM, 0.05mM, 0.1mM and 0.5mM) did not show the prominent cross linking of protein. Conclusion: Formaldehyde was found to be a more potent glycating agent compared to D-ribose. Compared to D-ribose, formaldehyde can produce protein misfolding and can be used in clinical research to establish the role of formaldehyde in patients with diseases.

Wild-type hen egg white lysozyme aggregation in vitro can form self-seeding amyloid conformational variants

2016 ◽  
Vol 219 ◽  
pp. 28-37 ◽  
Author(s):  
Vishwanath Sivalingam ◽  
Nalla Lakshmi Prasanna ◽  
Neetu Sharma ◽  
Archana Prasad ◽  
Basant K Patel
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Wild Type ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg ◽  
Lysozyme Aggregation

scholarly journals Molecular Dynamics Study on the Effects of Charged Amino Acid Distribution Under low pH Condition to the Unfolding of Hen Egg White Lysozyme and Formation of Beta Strands.

2021 ◽  
Author(s):  
Thana Sutthibutpong ◽  
Piyapong Asanithi ◽  
Ibra Alam ◽  
Husnul Fuad Zein
Keyword(s):  
Molecular Dynamics ◽  
Amyloid Fibrils ◽  
Egg White ◽  
Low Ph ◽  
Hen Egg White Lysozyme ◽  
Beta Strand ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Aggregation of unfolded or misfolded proteins into amyloid fibrils can cause various diseases in humans. However, the fibrils synthesized in vitro can be developed toward useful biomaterials under some physicochemical conditions. In this study, atomistic molecular dynamics simulations were performed to address the mechanism of beta-sheet formation of the unfolded hen egg white lysozyme (HEWL) under a high temperature and low pH. Simulations of the protonated HEWL at pH 2 and the non-protonated HEWL at pH 7 were performed at the highly elevated temperature of 450 K to accelerate the unfolding, followed by the 333 K temperature in some previous in vitro studies. The simulations showed that HEWL unfolded faster and refolded into structures with higher beta-strand contents at pH 2. The mechanism of beta-strand formation at the earlier stage of amyloidosis was addressed in terms of the radial distribution of amino acids, affected by the high protonation level at a low pH.

scholarly journals The impact of folding modes and deuteration on the atomic resolution structure of hen egg-white lysozyme

2021 ◽  
Vol 77 (12) ◽  
Author(s):  
Joao Ramos ◽  
Valerie Laux ◽  
Michael Haertlein ◽  
V. Trevor Forsyth ◽  
Estelle Mossou ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Egg White ◽  
Atomic Resolution ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
The Impact ◽  
Hen Egg

The biological function of a protein is intimately related to its structure and dynamics, which in turn are determined by the way in which it has been folded. In vitro refolding is commonly used for the recovery of recombinant proteins that are expressed in the form of inclusion bodies and is of central interest in terms of the folding pathways that occur in vivo. Here, biophysical data are reported for in vitro-refolded hydrogenated hen egg-white lysozyme, in combination with atomic resolution X-ray diffraction analyses, which allowed detailed comparisons with native hydrogenated and refolded perdeuterated lysozyme. Distinct folding modes are observed for the hydrogenated and perdeuterated refolded variants, which are determined by conformational changes to the backbone structure of the Lys97–Gly104 flexible loop. Surprisingly, the structure of the refolded perdeuterated protein is closer to that of native lysozyme than that of the refolded hydrogenated protein. These structural differences suggest that the observed decreases in thermal stability and enzymatic activity in the refolded perdeuterated and hydrogenated proteins are consequences of the macromolecular deuteration effect and of distinct folding dynamics, respectively. These results are discussed in the context of both in vitro and in vivo folding, as well as of lysozyme amyloidogenesis.

Inactivation of hen egg-white lysozyme. The azide radical

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg
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