Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.689913
Title: Host defence peptide (HDP) human beta defensin 9 (HBD9)
Author: Omar, Nazri
ISNI:       0000 0004 5921 2200
Awarding Body: University of Nottingham
Current Institution: University of Nottingham
Date of Award: 2016
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Abstract:
Introduction: The emergence of antibiotic resistance has led to the continuing search for discovery of effective antibiotics. Host defence peptides (HDPs) confer defence mechanisms against infection and investigation of their specific roles and interplays are ongoing. Among the HDPs, defensins are a group of effector molecules which plays important roles in humans. Although several stereotypes of human beta defensins (hBDs) such as the hBD1-3 are well studied, other members including the human beta defensin 9 (hBD9), are not entirely known. Understanding the properties of these HDPs will enable us to discover a safe and efficacious, broad-spectrum and resistance-free antibiotic for therapeutic application in the future. Purpose: The purpose of this study is to clone the DEFB109 gene, express and purify the hBD9 propeptide, before determining the hBD9 propeptide antimicrobial property using a recombinant system in Escherichia coli. Methods: The second exon of the DEFB109 was amplified through reverse transcription polymerase chain reaction (RT-PCR) and inserted into selected plasmid vectors. The recombinant plasmid construct was cloned, and transformed into E coli expression host. The correctly transformed colonies were selected before the plasmid constructs were purified and verified through nucleotide sequencing. Expression and purification of the hBD9 propeptide were carried out and antimicrobial property of the peptide was investigated. Result: HBD9 fusion protein was successfully expressed and purified. It was shown to have antimicrobial efficacy against Staphylococcus aureus and Pseudomonas aeruginosa. The effect of the free hBD9 propeptide against wider spectrum of organisms needs to be studied in the future.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.689913  DOI: Not available
Keywords: QU Biochemistry
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