Investigate the interaction of cationic polymers with bacteria through ITC

In order for cationic antimicrobial beta ( β) peptides to become a major force in tackling the problems of infectious disease that are caused by bacteria and virus, extensive studies and experiments have to be conducted to fully understand the working principle and working mechanism of it. As the st...

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Main Author: Yip, Feng Kai
Other Authors: Si Zhang Yong
Format: Final Year Project
Language:English
Published: 2018
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Online Access:http://hdl.handle.net/10356/75601
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-756012023-03-03T15:34:16Z Investigate the interaction of cationic polymers with bacteria through ITC Yip, Feng Kai Si Zhang Yong Chan Bee Eng, Mary School of Chemical and Biomedical Engineering DRNTU::Engineering::Bioengineering In order for cationic antimicrobial beta ( β) peptides to become a major force in tackling the problems of infectious disease that are caused by bacteria and virus, extensive studies and experiments have to be conducted to fully understand the working principle and working mechanism of it. As the structure of bacteria comprises of many complex materials, the experiments done on peptides and bacteria itself could lead to inaccurate results being acquired. Thus, simple bacteria model liposomes that resemble the structure of the bacteria itself are used in experiments with the cationic antimicrobial  peptides so that results of high precision and accuracy are obtained. This project reports the binding interaction between the cationic antimicrobial peptides 154-6 to the membrane of various bacteria model liposomes using Isothermal Titration Calorimetry (ITC). Cationic antimicrobial peptide 154-6 is a synthetic antimicrobial peptide designed to have better efficiency and selectivity as compared to naturally occurring antimicrobial peptides. Large unilamellar vesicles (LUVs) comprise of L-α-Phosphatidylcholine (POPC), 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-rac-(1-glycerol)] (POPG) and Lipopolysaccharides (LPS) from Escherichia coli (E coil), were used as model system for the membrane of Gram-negative bacteria, Gram-positive bacteria and mammalian cell. It was illustrated that the binding reaction between the peptides and the membrane models were exothermic and the reactions occurred were spontaneous and favourable as the product that was produced during the reaction was stable. It was also discovered that the binding affinity between the different types of membrane models and the peptides were different which leads to the difference in binding strength between the peptides and the different types of membrane models. Ultimately, the binding of the peptides to the membrane models could cause inhibition of cell wall synthesis in bacteria and eventually result in cell death in bacteria. Bachelor of Engineering (Chemical and Biomolecular Engineering) 2018-06-05T03:50:38Z 2018-06-05T03:50:38Z 2018 Final Year Project (FYP) http://hdl.handle.net/10356/75601 en Nanyang Technological University 43 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::Bioengineering
spellingShingle DRNTU::Engineering::Bioengineering
Yip, Feng Kai
Investigate the interaction of cationic polymers with bacteria through ITC
description In order for cationic antimicrobial beta ( β) peptides to become a major force in tackling the problems of infectious disease that are caused by bacteria and virus, extensive studies and experiments have to be conducted to fully understand the working principle and working mechanism of it. As the structure of bacteria comprises of many complex materials, the experiments done on peptides and bacteria itself could lead to inaccurate results being acquired. Thus, simple bacteria model liposomes that resemble the structure of the bacteria itself are used in experiments with the cationic antimicrobial  peptides so that results of high precision and accuracy are obtained. This project reports the binding interaction between the cationic antimicrobial peptides 154-6 to the membrane of various bacteria model liposomes using Isothermal Titration Calorimetry (ITC). Cationic antimicrobial peptide 154-6 is a synthetic antimicrobial peptide designed to have better efficiency and selectivity as compared to naturally occurring antimicrobial peptides. Large unilamellar vesicles (LUVs) comprise of L-α-Phosphatidylcholine (POPC), 1-Palmitoyl-2-Oleoyl-sn-Glycero-3-[Phospho-rac-(1-glycerol)] (POPG) and Lipopolysaccharides (LPS) from Escherichia coli (E coil), were used as model system for the membrane of Gram-negative bacteria, Gram-positive bacteria and mammalian cell. It was illustrated that the binding reaction between the peptides and the membrane models were exothermic and the reactions occurred were spontaneous and favourable as the product that was produced during the reaction was stable. It was also discovered that the binding affinity between the different types of membrane models and the peptides were different which leads to the difference in binding strength between the peptides and the different types of membrane models. Ultimately, the binding of the peptides to the membrane models could cause inhibition of cell wall synthesis in bacteria and eventually result in cell death in bacteria.
author2 Si Zhang Yong
author_facet Si Zhang Yong
Yip, Feng Kai
format Final Year Project
author Yip, Feng Kai
author_sort Yip, Feng Kai
title Investigate the interaction of cationic polymers with bacteria through ITC
title_short Investigate the interaction of cationic polymers with bacteria through ITC
title_full Investigate the interaction of cationic polymers with bacteria through ITC
title_fullStr Investigate the interaction of cationic polymers with bacteria through ITC
title_full_unstemmed Investigate the interaction of cationic polymers with bacteria through ITC
title_sort investigate the interaction of cationic polymers with bacteria through itc
publishDate 2018
url http://hdl.handle.net/10356/75601
_version_ 1759854397073915904