Inhibition of OmpT activity using D-amino acid peptides

Foodborne diseases such as food poison and diarrhoea are widespread in the world and it has led to many cases of hospitalisation and in extreme cases, death. One of its main causes is due to bacterial pathogens such Escherichia Coli (E. Coli) [1]. Anti-microbial peptides (AMPs) are secreted from epi...

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Main Author: Lim, Ernest Jun Wei
Other Authors: Bo Liedberg
Format: Final Year Project
Language:English
Published: Nanyang Technological University 2020
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Online Access:https://hdl.handle.net/10356/138794
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-1387942023-03-04T15:46:57Z Inhibition of OmpT activity using D-amino acid peptides Lim, Ernest Jun Wei Bo Liedberg School of Materials Science and Engineering Centre for Biomimetic Sensor Science bliedberg@ntu.edu.sg Engineering::Materials Foodborne diseases such as food poison and diarrhoea are widespread in the world and it has led to many cases of hospitalisation and in extreme cases, death. One of its main causes is due to bacterial pathogens such Escherichia Coli (E. Coli) [1]. Anti-microbial peptides (AMPs) are secreted from epithelial cells lining the host intestinal lumen to kill off the E. Coli pathogen [2]. However, OmpT is an outer membrane protease present on the surface of E. Coli membrane and that it acts as a defence mechanism against anti-microbial peptides by cleaving the AMPs [3]. In order to kills off the E. Coli effective, an inhibitor is required to slow down or stop OmpT activity. One possible way to inhibit OmpT activity is through the use of D-amino acid peptides. D-amino acid peptides are stereoisomer from the more commonly found L-amino acids. These peptides are more resistant to degradation and are not cleaved by OmpT [4]. As such this report aims to investigate whether D-amino acid peptide can be developed into inhibitors of OmpT activity. Bachelor of Engineering (Materials Engineering) 2020-05-12T11:06:33Z 2020-05-12T11:06:33Z 2020 Final Year Project (FYP) https://hdl.handle.net/10356/138794 en application/pdf Nanyang Technological University
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Engineering::Materials
spellingShingle Engineering::Materials
Lim, Ernest Jun Wei
Inhibition of OmpT activity using D-amino acid peptides
description Foodborne diseases such as food poison and diarrhoea are widespread in the world and it has led to many cases of hospitalisation and in extreme cases, death. One of its main causes is due to bacterial pathogens such Escherichia Coli (E. Coli) [1]. Anti-microbial peptides (AMPs) are secreted from epithelial cells lining the host intestinal lumen to kill off the E. Coli pathogen [2]. However, OmpT is an outer membrane protease present on the surface of E. Coli membrane and that it acts as a defence mechanism against anti-microbial peptides by cleaving the AMPs [3]. In order to kills off the E. Coli effective, an inhibitor is required to slow down or stop OmpT activity. One possible way to inhibit OmpT activity is through the use of D-amino acid peptides. D-amino acid peptides are stereoisomer from the more commonly found L-amino acids. These peptides are more resistant to degradation and are not cleaved by OmpT [4]. As such this report aims to investigate whether D-amino acid peptide can be developed into inhibitors of OmpT activity.
author2 Bo Liedberg
author_facet Bo Liedberg
Lim, Ernest Jun Wei
format Final Year Project
author Lim, Ernest Jun Wei
author_sort Lim, Ernest Jun Wei
title Inhibition of OmpT activity using D-amino acid peptides
title_short Inhibition of OmpT activity using D-amino acid peptides
title_full Inhibition of OmpT activity using D-amino acid peptides
title_fullStr Inhibition of OmpT activity using D-amino acid peptides
title_full_unstemmed Inhibition of OmpT activity using D-amino acid peptides
title_sort inhibition of ompt activity using d-amino acid peptides
publisher Nanyang Technological University
publishDate 2020
url https://hdl.handle.net/10356/138794
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