Parallel β-Sheet Fibril and Antiparallel β-Sheet Oligomer: New Insights into Amyloid Formation of Hen Egg White Lysozyme under Heat and Acidic Condition from FTIR Spectroscopy

2013 ◽  
Vol 117 (15) ◽  
pp. 4003-4013 ◽  
Author(s):  
Ye Zou ◽  
Yiyi Li ◽  
Wenying Hao ◽  
Xiaoqian Hu ◽  
Gang Ma
Keyword(s):  
Ftir Spectroscopy ◽  
Egg White ◽  
Acidic Condition ◽  
Amyloid Formation ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Β Sheet ◽  
Hen Egg

scholarly journals Ethanol-induced amyloid formation of hen egg-white lysozyme : a small-angle X-ray scattering study

2000 ◽  
Vol 40 (supplement) ◽  
pp. S115
Author(s):  
Y. Yonezawa ◽  
S. Tanaka ◽  
T. Kubota ◽  
K. Wakabayashi ◽  
K. Yutani ◽  
...  
Keyword(s):  
Small Angle ◽  
Egg White ◽  
Amyloid Formation ◽  
Hen Egg White Lysozyme ◽  
X Ray ◽  
Egg White Lysozyme ◽  
X Ray Scattering ◽  
Scattering Study ◽  
Hen Egg White ◽  
Hen Egg

Methylation at lysine side chain of hen egg white lysozyme (HEWL) promote its amyloid formation

2011 ◽  
Vol 44 (13) ◽  
pp. S23-S24
Author(s):  
Ostadi Hassan ◽  
Shariat Sajjad ◽  
Ali Akbar Meratan ◽  
Ali Es-haghi ◽  
Mohsen Nemat-Gorgani
Keyword(s):  
Egg White ◽  
Side Chain ◽  
Amyloid Formation ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Lysine Side Chain ◽  
Hen Egg White ◽  
Hen Egg

Inhibitory as well as disaggregation potential of selected hydroxy benzoic phytochemicals on hen egg white lysozyme amyloidogenesis

2020 ◽  
Vol 17 ◽  
Author(s):  
Nandini Sarkar ◽  
Vidyalatha Kolli ◽  
Taraka Prabhu MP ◽  
Arbin Basak ◽  
Hitesh Mandal
Keyword(s):  
Conformational Changes ◽  
Vanillic Acid ◽  
Egg White ◽  
Cd Spectroscopy ◽  
Docking Studies ◽  
Amyloid Formation ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Background: Amyloids are a class of ordered protein aggregates which have been implicated in the onset of several degenerative diseases such as Alzheimer's disease, Parkinson's disease, Type II diabetes and so on. Despite extensive research, the exact mechanism and the driving factors for the amyloidogenesis process remain elusive. Identifying molecules which can effectively inhibit and/or disaggregate the fibrils may be one effective therapeutic strategy against amyloidosis Objectives: In the current study, few hydroxy-benzoic phytochemicals were selected to study their effects on formation as well as disaggregation of hen egg white lysozyme (HEWL) amyloids, namely gallic acid, syringic acid, vanillic acid and iso-vanillic acid. Method: Amyloidogenesis was monitored using methods like the thioflavin T assay, field emission scanning electron mi-croscopy (FESEM) and dynamic light scattering (DLS) studies. Further protein conformational changes were monitored us-ing methods like 8-Anilino-naphthalene-1-sulfonate (ANS) fluorescence, circular dichroism (CD) spectroscopy and guani-dine hydrochloride mediated stability studies. Computational approach was also employed to get an insight on the interac-tion(s) between the selected compounds and HEWL using docking studies Result: The selected compounds exhibited significant inhibitory as well as disaggregation effects on HEWL amyloids. In-teraction with the phytochemicals was also associated with considerable conformational changes in HEWL. Docking studies show role of hydrogen bonding between HEWL and the phytochemicals. Conclusion: Thus the current study throws light on the key factors that drive amyloid formation and hence will be helpful for development of effective therapeutics against amyloidosis.

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