Expression studies on antimicrobial protein, human beta defensin 25 fused with GST

Expression studies on antimicrobial protein, human beta defensin 25 fused with GST

Human β-Defensin 25 (HBD-25) is a novel cationic antimicrobial peptide found in high abundance in male genital tract. The broad spectra of the antimicrobial activity of HBD against microbes make it a potential therapeutic agent in treatment against increasing antibiotic resistance in humans towards...

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Main Author: Er, Clarice Ru Hui
Other Authors: Susanna Leong Su Jan
Format: Final Year Project
Language:English
Published: 2009
Subjects:
DRNTU::Engineering::Chemical engineering::Biotechnology
Online Access:http://hdl.handle.net/10356/16392
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-163922023-03-03T15:41:33Z Expression studies on antimicrobial protein, human beta defensin 25 fused with GST Er, Clarice Ru Hui Susanna Leong Su Jan School of Chemical and Biomedical Engineering DRNTU::Engineering::Chemical engineering::Biotechnology Human β-Defensin 25 (HBD-25) is a novel cationic antimicrobial peptide found in high abundance in male genital tract. The broad spectra of the antimicrobial activity of HBD against microbes make it a potential therapeutic agent in treatment against increasing antibiotic resistance in humans towards bacteria infection. Therefore, the expression of high yield and purity of HBD-25 using Ecoli as host cells will be desirable in order to facilitate clinical studies on HBD-25. The harmful effects of the expression of HBD-25 on the Ecoli had been avoided by attaching a fusion tag to the N-terminal of HBD-25. Glutathione S-Transferase (GST) is selected as the fusion tag to enhance the solubility of fusion protein.In this project, the expression conditions required for high yield and purity of GST-HBD-25 were investigated. Bachelor of Engineering (Chemical and Biomolecular Engineering) 2009-05-26T02:36:36Z 2009-05-26T02:36:36Z 2009 2009 Final Year Project (FYP) http://hdl.handle.net/10356/16392 en Nanyang Technological University 49 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Engineering::Chemical engineering::Biotechnology
spellingShingle DRNTU::Engineering::Chemical engineering::Biotechnology
Er, Clarice Ru Hui
Expression studies on antimicrobial protein, human beta defensin 25 fused with GST
description Human β-Defensin 25 (HBD-25) is a novel cationic antimicrobial peptide found in high abundance in male genital tract. The broad spectra of the antimicrobial activity of HBD against microbes make it a potential therapeutic agent in treatment against increasing antibiotic resistance in humans towards bacteria infection. Therefore, the expression of high yield and purity of HBD-25 using Ecoli as host cells will be desirable in order to facilitate clinical studies on HBD-25. The harmful effects of the expression of HBD-25 on the Ecoli had been avoided by attaching a fusion tag to the N-terminal of HBD-25. Glutathione S-Transferase (GST) is selected as the fusion tag to enhance the solubility of fusion protein.In this project, the expression conditions required for high yield and purity of GST-HBD-25 were investigated.
author2 Susanna Leong Su Jan
author_facet Susanna Leong Su Jan
Er, Clarice Ru Hui
format Final Year Project
author Er, Clarice Ru Hui
author_sort Er, Clarice Ru Hui
title Expression studies on antimicrobial protein, human beta defensin 25 fused with GST
title_short Expression studies on antimicrobial protein, human beta defensin 25 fused with GST
title_full Expression studies on antimicrobial protein, human beta defensin 25 fused with GST
title_fullStr Expression studies on antimicrobial protein, human beta defensin 25 fused with GST
title_full_unstemmed Expression studies on antimicrobial protein, human beta defensin 25 fused with GST
title_sort expression studies on antimicrobial protein, human beta defensin 25 fused with gst
publishDate 2009
url http://hdl.handle.net/10356/16392
_version_ 1759858404669521920

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