Camesano, Terri Anne
Bacterial infections from contaminated food and medical devices are a common occurrence. Antimicrobial peptides (AMPs) effectively kill bacteria in solution. Peptides immobilized to a surface with a flexible spacer molecule, such as SM(PEG)12, may allow the peptides to retain their antibacterial properties, potentially helping to prevent these bacterial infections. This study focused on determining the ability of immobilized Chrysophsin-1, an AMP, to kill S. aureus, a gram-positive bacterium. QCM-D was used to characterize peptide and bacterial adsorption to a SiO2 surface. Results showed that Chrysophsin-1 bound via an SM(PEG)12 spacer molecule were not as effective at killing S. aureus when compared to peptide that was physically adsorbed to the surface.
Worcester Polytechnic Institute
Major Qualifying Project
All authors have granted to WPI a nonexclusive royalty-free license to distribute copies of the work, subject to other agreements. Copyright is held by the author or authors, with all rights reserved, unless otherwise noted.