Effect of Polyethylene Oxide (PEO) Modification on the Structure and Antimicrobial Activity of the Antimicrobial Peptide WLBU2 Public

http://ir.library.oregonstate.edu/concern/honors_college_theses/n296x117k

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  • Sepsis is a blood infection that is caused by circulating bacteria cells and cell fragments, which contain immunogenic lipopolysaccharides (LPS) or endotoxin. The circulating endotoxin results in a severe dysregulation of the inflammatory response that ultimately leads to organ failure. One promising treatment method is removal of endotoxin by passing blood through a high-throughput, microfluidic device coated with polyethylene oxide (PEO) and antimicrobial cationic amphiphilic peptide WLBU2. A critical step in the development of this microfluidic device is to demonstrate that PEGylation of WLBU2 at the N-terminal group does not negatively affect WLBU2’s LPS-binding and antimicrobial activity. Verification of successful PEGylation was performed using gel permeation chromatography (GPC). Secondary structure changes were monitored using circular dichroism (CD), which concluded that the WLBU2 in all PEO-WLBU2 conjugates (5, 10, 20, and 30 kDa) was still able to adopt an α-helical structure in the presence of LPS. Antimicrobial activity was assessed using a liquid kinetic assay against E. coli, which illustrated that WLBU2 in the conjugates was able to maintain some antimicrobial activity after PEO-modification. The results of this project suggest that attachment of a PEO tether to WLBU2 is a feasible method for further attachment to the proposed microfluidic device surface. Key Words: Cationic amphiphilic peptides (CAPs), antimicrobial peptides, polyethylene oxide (PEO), PEGylation, peptide structure, circular dichroism (CD), gel permeation chromatography (GPC)
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