Modulation of Protein Amyloidogenicity by heterologous amyloid and post translational modification

Manglunia, Ruchi Rajkumar (2017) Modulation of Protein Amyloidogenicity by heterologous amyloid and post translational modification. Masters thesis, Indian Institute of Technology Hyderabad.

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Protein misfolding and aggregation in cells and serum is affected by many factors. Two of the factors studied here are: presence of heterologous aggregating protein in the cell and modification of protein by post translational modification. The effect of heterologous protein TDP-43 has been shown on PolyQ103-GFP protein. Huntington’s Disease patients’ brain have shown the presence of TDP-43 aggregates along with htt (PolyQ103-GFP) protein aggregates. Thus, we propose the reason for its presence could be enhancement of the primary protein. Alongside, it is also shown that PolyQ103-GFP protein may be independent of yeast prion for its aggregation in yeast strains. The effect of post translational modification, acetylation, has been studied on HSA structure and its amyloid forming ability. Aspirin is known to cause a permanent acetylation of HSA. Aspirin is used on a large scale by a large population and is known to cause many pathological conditions. Thus, its effects are studied on one of the most abundantly found serum protein, HSA. We found, the structure of HSA is affected by acetylation and so are its amyloid forming abilities. Acetylation attenuates HSA amyloidosis and distorts its structure. Further work on the same will provide deeper insights on the effects of aspirin on HSA.

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IITH Creators:
IITH CreatorsORCiD
Item Type: Thesis (Masters)
Uncontrolled Keywords: PolyQ, TDP-43, Acetylation, HSA, amyloidosis, TD826
Subjects: Others > Biotechnology
Divisions: Department of Biotechnology
Depositing User: Team Library
Date Deposited: 27 Jun 2017 11:28
Last Modified: 27 Jun 2017 11:28
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