Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes

Konstantin Andreev, Michael W. Martynowycz, Mia L. Huang, Ivan Kuzmenko, Wei Bu, Kent Kirshenbaum, David Gidalevitz

Research output: Contribution to journalArticlepeer-review


Hydrophobic interactions govern specificity for natural antimicrobial peptides. No such relationship has been established for synthetic peptoids that mimic antimicrobial peptides. Peptoid macrocycles synthesized with five different aromatic groups are investigated by minimum inhibitory and hemolytic concentration assays, epifluorescence microscopy, atomic force microscopy, and X-ray reflectivity. Peptoid hydrophobicity is determined using high performance liquid chromatography. Disruption of bacterial but not eukaryotic lipid membranes is demonstrated on the solid supported lipid bilayers and Langmuir monolayers. X-ray reflectivity studies demonstrate that intercalation of peptoids with zwitterionic or negatively charged lipid membranes is found to be regulated by hydrophobicity. Critical levels of peptoid selectivity are demonstrated and found to be modulated by their hydrophobic groups. It is suggested that peptoids may follow different optimization schemes as compared to their natural analogues.

Original languageEnglish (US)
Pages (from-to)1414-1423
Number of pages10
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number6
StatePublished - Jun 2018


  • AFM
  • Antimicrobial peptoids
  • Cytotoxicity
  • Hydrophobicity
  • Lipid membranes
  • X-ray scattering

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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