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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Bannon, Christopher Jeffrey
• Tongue, Kathryn Grace
• Skelton, Emily Anne

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-041713-135221

Advisor

• Camesano, Terri Anne

Year

• 2013

Date created

• 2013-04-17

Ort

• Nancy

Resource type

• Major Qualifying Project

Major

• Chemical Engineering

Rights statement

• In Copyright