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Permanent link (DOI): https://doi.org/10.7939/R3RT2Q

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Engineering Surface-tethered Bacteriocins for Studying Peptide-bacteria Interactions Open Access

Descriptions

Other title
Subject/Keyword
Peptide-immobilizatios
Leucocin A
Peptide-bacteria Interactions
Antimicrobial Peptides; Leucocin A; Peptide-Immobilization; Peptide-bacteria Interactions
Antimicrobial Peptides
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Etayash, Hashem Ra
Supervisor and department
Kamaljit Kaur
Examining committee member and department
Dr. Lavasanifar, Dr. Carlos Velázquez and Dr. Thomas Thundat
Dr. Thomas Thundat “Canada Excellence Research Chair, CERC”, Department
Dr. Lavasanifar, Faculty of Pharmacy and Pharmaceutical Sciences
Dr. Carlos Velázquez, Faculty of Pharmacy and Pharmaceutical Sciences
Department
Faculty of Pharmacy and Pharmaceutical Sciences
Specialization
Pharmaceutical Sciences
Date accepted
2012-10-19T14:30:25Z
Graduation date
2013-06
Degree
Master of Science
Degree level
Master's
Abstract
Identification and quantification of pathogenic bacteria has become one of the key elements in biodefense, food safety, diagnostic and drug discovery. The aim of the thesis is to investigate interactions between bacteria and peptides in order to utilize the potential of antimicrobial peptides (AMPs) in specific recognition of pathogenic bacteria. Leucocin A (LeuA) is an AMP that exhibits specific activity against L. monocytogenes at nanomolar concentrations. Here, we have synthesized full length LeuA and a shorter fragment using solid phase peptide synthesis. The peptides were characterized and individually immobilized on gold substrate. The bacterial specificity of the anchored peptides was tested against various strains and the results reveal that the adsorbed AMPs display significant binding towards Gram-positive bacteria with various binding affinities from one strain to another. Further, molecular dynamics simulation studies were conducted to provide atomistic insight on the mechanism of peptide-peptide and peptide lipid interactions in a membrane mimicking environment.
Language
English
DOI
doi:10.7939/R3RT2Q
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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