- Title
- In Silico analysis of Spermidine, Spermine and Putrescine interaction with selected heat shock proteins from Plasmodium falciparum 3D7 towards malaria drug development
- Creator
- Godlo, Sesethu
- Subject
- Heat shock proteins
- Subject
- Malaria vaccine
- Subject
- Plasmodium falciparum
- Date
- 2022
- Type
- Master'stheses
- Type
- text
- Identifier
- http://hdl.handle.net/10353/27709
- Identifier
- vital:69395
- Description
- Malaria is a mosquito-borne disease that affects around half of the world's population. It is one of the most common parasite infections that endangers human life. One of the most serious issues in malaria therapy is the emergence and spread of antimalarial drug-resistant Plasmodium parasites. This is due to the Plasmodium parasite's constant evolution and development of new methods of surviving medication toxicity. Studies of antimalarial drug development have been focused on polyamine biosynthesis by targeting precursors such as ornithine decarboxylase, adenosylmethionine decarboxylase, and spermidine synthase and protein-protein interactions between Plasmodium falciparum chaperones spotting out Hsp90, Hsp70, and Hsp40 as potential targets with little attention being paid to the interaction between polyamines and molecular chaperones. Therefore, this study seeks to identify interactions between polyamines and molecular chaperones present in the malarial parasite Plasmodium falciparum 3D7. The identification of these interactions might lead to the design of effective drugs to treat and eliminate malaria. Using computational analysis, this study aims to find interactions between polyamines and molecular chaperones found in the malarial parasite Plasmodium falciparum 3D7. The sequences of the selected heat proteins retrieved, and the 3D structures predicted and validated. These structures were docked with polyamines retrieved from PubChem and MD simulations on the docked interactions were performed. Docking revealed common amino acid residues with hydrogen bonds and salt bridges between all receptors and ligands, with glutamine and aspartic acid standing out. MD simulations revealed that when HSP20 and HSP40 transport the ligands, they pop up or are released too quickly. However, HSP60, HSP70, and HSP90 provide optimism since the ligands remain attached to the proteins for a specific amount of time. To further understand and confirm these interactions wet laboratory studies may be carried out in future.
- Description
- Thesis (MSci) -- Faculty of Science and Agriculture, 2022
- Format
- computer
- Format
- online resource
- Format
- application/pdf
- Format
- 1 online resource (xi, 104 leaves)
- Format
- Publisher
- University of Fort Hare
- Publisher
- Faculty of Science and Agriculture
- Language
- English
- Rights
- University of Fort Hare
- Rights
- All Rights Reserved
- Rights
- Open Access
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UFH Department of Biochemistry & Microbiology
| Thumbnail | File | Description | Size | Format | |||
|---|---|---|---|---|---|---|---|
| View Details Download | SOURCE1 | MSc dissertation-Godlo-201715757.pdf | 4 MB | Adobe Acrobat PDF | View Details Download |