Alexander F. Chu-Kung

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The rise of resistant bacteria has prompted the search for new antimicrobial agents. Antimicrobial membrane lytic peptides have potential as future microbial agents due to their novel mode of action. Recently conjugation of a fatty acid to antimicrobial peptides has been explored as a method to modulate the activity and selectivity of the peptide. Our work(More)
Two peptides, YGAA[KKAAKAA]2 (AKK), and YG[AKAKAAKA]2 (KAK) were conjugated to fatty acids and tested for the effect on their structure, antibacterial activity, and eukaryotic cell toxicity. In the presence of bacteria-mimicking phospholipid vesicles fatty acid conjugates of the amphipathic peptide, AKK, show a larger change in helical structure than either(More)
Three peptides, YGAA[KKAAKAA](2) (AKK), KLFKRHLKWKII (SC4), and YG[AKAKAAKA](2) (KAK), were conjugated with lauric acid and tested for the effect on their structure, antibacterial activity, and eukaryotic cell toxicity. The conjugated AKK and SC4 peptides showed increased antimicrobial activity relative to unconjugated peptides, but the conjugated KAK(More)
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