Arakha, Manoranjan (2012)
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Abstract
Protein
misfolding and aggregation are responsible for several human
pathologies commonly known as protein misfolding diseases. The various
examples of protein misfolding diseases are: Alzheimer disease,
spongiform encephalopathy, diabetes type 2, serpin-deficiency disorder,
Huntington disease, Parkinson disease, amyloid polyneuropathy, and
several others. The current research work was carried out to investigate
the potential of ZnO nanoparticle to prevent lysozyme aggregation. ZnO
nanoparticles were synthesized by chemical precipitation method from
Zinc acetate dihydrate and urea. The optical, morphological and
structural properties of synthesized ZnO nanoparticles have been studied
using UV-Vis spectrophotometer, SEM, DLS, XRD and EDS. UV-Vis
spectroscopic study shows that ZnO nanoparticles have surface plasmon
resonance at 375nm. DLS analysis shows the average size of synthesized
ZnO nanoparticle to be 68 nm. The EDS analysis shows the elemental
composition of synthesized ZnO naoparticles and XRD study confirms the
wurtzite structure of ZnO nanoparticles. The lysozyme aggregation was
prepared by heating the native lysozyme at 1000C. The effect of ZnO
nanoparticles on the aggregation of lysozyme was studied. DLS analysis
shows the mean size of the aggregates decreases with increasing
concentration of ZnO nanoparticle (NP), which was further confirmed by
SEM analysis. UV-Vis and Fluorescence spectroscopic studies were
performed to analyze the structural changes of lysozyme upon binding
with nanoparticles. The Congo red assay was performed to study the
formation of amyloid fibrils.
Item Type: | Thesis (MTech) |
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Uncontrolled Keywords: | Protein misfolding, Aggregation, Nanoparticles, Zinc oxide, Congo red assay |
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