Engineering Surface-tethered Bacteriocins for Studying Peptide-bacteria Interactions

• Author / Creator

  Etayash, Hashem Ra

• 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.

• Subjects / Keywords

  • Peptide-bacteria Interactions
  • Peptide-immobilizatios
  • Antimicrobial Peptides; Leucocin A; Peptide-Immobilization; Peptide-bacteria Interactions
  • Leucocin A
  • Antimicrobial Peptides

• Graduation date

  Spring 2013

• Type of Item

  Thesis

• Degree

  Master of Science

• DOI

  https://doi.org/10.7939/R3RT2Q

• License

  This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.