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Peptide inhibitors targeting amyloid beta and tau as potential therapeutics for Alzheimer’s disease
- Author(s)
- 김예린
- Advisor
- 서민덕
- Department
- 일반대학원 분자과학기술학과
- Publisher
- The Graduate School, Ajou University
- Publication Year
- 2023-02
- Language
- eng
- Keyword
- Alzheimer's disease; Peptide inhibitor; amyloid beta; tau
- Alternative Abstract
- The mechanism and cause of neurodegenerative diseases, including Alzheimer’s disease, Parkinson's disease, and Huntington’s disease, are not yet known. Various cellular changes, including the production and accumulation of amyloid beta (Aβ), the formation and accumulation of phosphorylated tau, have been found to be involved in the occurrence of Alzheimer’s disease. Neuritic plaques and neurofibrillary tangles are observed in brain tissues of people with neurodegenerative diseases, and brain atrophy due to nerve cell loss is also found. <br>Aβ is a peptide derived from the amyloid precursor protein (APP), a major component of amyloid plaque found in the brain of Alzheimer’s patients. Aβ molecules can aggregate to oligomers that cans exist in various forms. Tau proteins are essentially unfolded state and contribute to microtubule assembly and stabilization in our body. In pathological conditions, tau leads to the accumulation of toxic amyloid aggregates, which are involved in regression and neurodegenerative death associated with neurodegenerative diseases and can be reversed while inhibiting expression or aggregation. <br>Here, we investigated through Nuclear Magnetic Resonance (NMR), Thioflavin T (ThT) and Transmission electron microscopy (TEM) whether peptides are involved in the fibrillation process of Aβ/Tau protein and whether they inhibit fibrillation. Our analysis revealed that the peptides are involved in the fibrillation process of Aβ/Tau protein and inhibit fibril formation. In addition, the evaluation of the Aβ cytotoxicity inhibitory activity was tested at in vivo, and all four peptides were confirmed to specifically restore cytotoxicity.
- Fulltext
- Appears in Collections:
- Graduate School of Ajou University > Department of Molecular Science and Technology > 3. Theses(Master)
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