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...

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Main Author:	Soong, Jia Xin
Format:	Thesis
Language:	English
Published:	2018
Subjects:	R735-854 Medical education Medical schools Research
Online Access:	http://eprints.usm.my/44132/1/SOONG%20JIA%20XIN.pdf
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id	my-usm-ep.44132
record_format	uketd_dc
spelling	my-usm-ep.441322019-04-18T06:47:23Z In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis 2018-03 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 http://eprints.usm.my/44132/ http://eprints.usm.my/44132/1/SOONG%20JIA%20XIN.pdf application/pdf en public masters Universiti Sains Malaysia Institut Penyelidikan Perubatan Molekul
institution	Universiti Sains Malaysia
collection	USM Institutional Repository
language	English
topic	R735-854 Medical education Medical schools Research
spellingShingle	R735-854 Medical education Medical schools Research Soong, Jia Xin In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis
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.
format	Thesis
qualification_level	Master's degree
author	Soong, Jia Xin
author_facet	Soong, Jia Xin
author_sort	Soong, Jia Xin
title	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_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_sort	in silico optimisation of domain antibodies against hsp16.3 from mycobacterium tuberculosis
granting_institution	Universiti Sains Malaysia
granting_department	Institut Penyelidikan Perubatan Molekul
publishDate	2018
url	http://eprints.usm.my/44132/1/SOONG%20JIA%20XIN.pdf
_version_	1747821333619671040

In Silico Optimisation Of Domain Antibodies Against HSP16.3 From Mycobacterium Tuberculosis

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