Journal
CHEMMEDCHEM
Volume 7, Issue 1, Pages 114-122Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cmdc.201100358
Keywords
antibiotic resistance; antimicrobial peptides; foldamers; macrocycles; peptidomimetics
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Funding
- American Heart Association [10PRE3420022]
- New York University School of Medicine
- NSF [CHE-0645361]
- NIH [C060RR-165720]
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We investigated the antimicrobial activities of N-substituted glycine peptoid oligomers incorporating cationic and hydrophobic side chains. Head-to-tail macrocyclization was employed to enhance antimicrobial activity. Both linear and cyclic peptoids, ranging from six to ten residues, demonstrate potent antimicrobial activity against Gram-positive and Gram-negative bacteria. These peptoids do not cause significant lysis of human erythrocytes, indicating selective antimicrobial activity. Conformational ordering established upon macrocyclization is generally associated with an enhanced capacity to inhibit bacterial cell growth. Moreover, increased hydrophobic surface area also plays a role in improving antimicrobial activity. We demonstrate the potency of a cyclic peptoid in exerting antimicrobial activity against clinical strains of S. aureus while deterring the emergence of antimicrobial resistance.
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