Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides

Antimicrobial peptides (AMPs) and their mimics are emerging as promising antibiotic agents. We present a library of "ampetoids" (antimicrobial peptoid oligomers) with helical structures and biomimetic sequences, several members of which have low-micromolar antimicrobial activities, similar to cationic AMPs like pexiganan. Broad-spectrum activity against six clinically relevant BSL2 pathogens is also shown. This comprehensive structure-activity relationship study, including circular dichroism spectroscopy, minimum inhibitory concentration assays, hemolysis and mammalian cell toxicity studies, and specular x-ray reflectivity measurements shows that the in vitro activities of ampetoids are strikingly similar to…

• NS
  National Science Foundation

  Awards: DE-AC02-05CH11231, 0404704
• UD
  U.S. Department of Energy

  Awards: -AC02-05CH11231, 05CH11231, Contract DE-AC02-05CH11231, AC02-05CH11231, DE-AC02, DE-AC02-05CH11231, DE-AC02-
• UD
  U.S. Department of Homeland Security

  Awards: DE-AC02-05CH11231, AC02-05CH11231
• CA
  Camille and Henry Dreyfus Foundation
• NU
  Northwestern University
• NI
  National Institutes of Health

  Award: DE-AC02-05CH11231
• OO
  Office of Science

  Awards: Contract DE-AC02-05CH11231, AC02-05CH11231, -AC02-05CH11231, DE-AC02
• DO
  Division of Chemistry

  Awards: DE-AC02-05CH11231, CHE-0404704
• BE
  Basic Energy Sciences

  Awards: DE-AC02, AC02-05CH11231, DE-AC02-05CH11231, -AC02-05CH11231, Contract DE-AC02-05CH11231