In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis
Heat shock protein 16.3 (HSP16.3) from Mycobacterium tuberculosis (Mtb) is critical for its survival during latent infection in human, thus making it an attractive target for developing diagnostic and therapeutic strategies. The predicted structure of HSP16.3 was docked against a known HSP hydrophob...
| Main Author: | |
|---|---|
| Format: | Thesis |
| Language: | English |
| Published: |
2018
|
| Subjects: | |
| Online Access: | http://eprints.usm.my/44132/ http://eprints.usm.my/44132/1/SOONG%20JIA%20XIN.pdf |
| _version_ | 1848879982748631040 |
|---|---|
| author | Soong, Jia Xin |
| author_facet | Soong, Jia Xin |
| author_sort | Soong, Jia Xin |
| building | USM Institutional Repository |
| collection | Online Access |
| description | Heat shock protein 16.3 (HSP16.3) from Mycobacterium tuberculosis (Mtb) is critical for its survival during latent infection in human, thus making it an attractive target for developing diagnostic and therapeutic strategies. The predicted structure of HSP16.3 was docked against a known HSP hydrophobic probe, namely 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid (bisANS) and to the comparative models of HSP16.3 specific single domain antibodies (sdAbs), clone E3 and F1. The binding interactions were further elucidated by free energy calculations. The non-polar interactions were identified as the main force for antigen-antibody association. |
| first_indexed | 2025-11-15T17:55:53Z |
| format | Thesis |
| id | usm-44132 |
| institution | Universiti Sains Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T17:55:53Z |
| publishDate | 2018 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | usm-441322019-04-18T06:47:23Z http://eprints.usm.my/44132/ In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis Soong, Jia Xin R735-854 Medical education. Medical schools. Research Heat shock protein 16.3 (HSP16.3) from Mycobacterium tuberculosis (Mtb) is critical for its survival during latent infection in human, thus making it an attractive target for developing diagnostic and therapeutic strategies. The predicted structure of HSP16.3 was docked against a known HSP hydrophobic probe, namely 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid (bisANS) and to the comparative models of HSP16.3 specific single domain antibodies (sdAbs), clone E3 and F1. The binding interactions were further elucidated by free energy calculations. The non-polar interactions were identified as the main force for antigen-antibody association. 2018-03 Thesis NonPeerReviewed application/pdf en http://eprints.usm.my/44132/1/SOONG%20JIA%20XIN.pdf Soong, Jia Xin (2018) In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis. Masters thesis, Universiti Sains Malaysia. |
| spellingShingle | R735-854 Medical education. Medical schools. Research Soong, Jia Xin In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis |
| title | In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis |
| title_full | In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis |
| title_fullStr | In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis |
| title_full_unstemmed | In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis |
| title_short | In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis |
| title_sort | in silico optimisation of domain antibodies against hsp16.3 from mycobacterium tuberculosis |
| topic | R735-854 Medical education. Medical schools. Research |
| url | http://eprints.usm.my/44132/ http://eprints.usm.my/44132/1/SOONG%20JIA%20XIN.pdf |