Expression, purification, and characterization of putative choline kinases from microorganisms
| dc.contributor.author | Khalifa, Moad Mahmoud Alarabi | |
| dc.date.accessioned | 2020-12-14T07:12:11Z | |
| dc.date.available | 2020-12-14T07:12:11Z | |
| dc.date.issued | 2020-09 | |
| dc.description.abstract | yields compared to His-tagged proteins produced from the pET14b vector. Molecular docking of SaChoK, NmChoK, and HiChoK model structures with Hemicholinium-3 (HC-3), an established small-molecule ChoKI, exhibited a fit binding mode inside the choline-binding pocket, indicating promising competitive inhibition by HC-3. Superimpositions of the three bacterial ChoK model structures with human ChoK revealed an ample homology, further supporting the use of ChoKIs previously used to inhibit human ChoK on AMR bacteria. The production of pGEX-SaChoK and the bioinformatic predictions have laid the groundwork for optimal overexpression of SaChoK, NmChoK, and HiChoK in E. coli system. The molecular docking results demonstrate the promising application of ChoKIs to combat AMR. Therefore, this study has paved the way towards successful overexpression of soluble recombinant bacterial ChoKs to be tested with currently available ChoKIs and reveal the potential of these compounds as antimicrobial agents. | en_US |
| dc.identifier.uri | http://hdl.handle.net/123456789/10766 | |
| dc.language.iso | en | en_US |
| dc.publisher | Pusat Pengajian Sains Perubatan, Universiti Sains Malaysia | en_US |
| dc.subject | Antimicrobial resistance (AMR) | en_US |
| dc.title | Expression, purification, and characterization of putative choline kinases from microorganisms | en_US |
| dc.type | Thesis | en_US |
Files
License bundle
1 - 1 of 1
Loading...
- Name:
- license.txt
- Size:
- 1.71 KB
- Format:
- Item-specific license agreed upon to submission
- Description: