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Title: Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes

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, epi-fluorescence 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. In conclusion, it is suggested that peptoids may follow different optimization schemes as compared to their natural analogues.
Authors:
 [1] ;  [2] ;  [3] ;  [4] ;  [5] ;  [6] ;  [7]
  1. Illinois Inst. of Technology, Chicago, IL (United States); Northwestern Univ., Evanston, IL (United States)
  2. Illinois Inst. of Technology, Chicago, IL (United States); Argonne National Lab. (ANL), Lemont, IL (United States); Howard Hughes Medical Institute, Ashburn, VA (United States)
  3. New York Univ., New York, NY (United States); Univ. of California-San Diego, La Jolla, CA (United States)
  4. Argonne National Lab. (ANL), Lemont, IL (United States)
  5. Univ. of Chicago, Chicago, IL (United States)
  6. New York Univ., New York, NY (United States)
  7. Illinois Inst. of Technology, Chicago, IL (United States)
Publication Date:
Grant/Contract Number:
AC02-06CH11357
Type:
Accepted Manuscript
Journal Name:
Biochimica et Biophysica Acta. Biomembranes
Additional Journal Information:
Journal Volume: 1860; Journal Issue: 6; Journal ID: ISSN 0005-2736
Publisher:
Elsevier
Research Org:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org:
National Science Foundation (NSF); National Institutes of Health (NIH); USDOE
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Antimicrobial peptoids; Lipid membranes; Cytotoxicity; AFM; Hydrophobicity; X-ray scattering
OSTI Identifier:
1472076

Andreev, Konstantin, Martynowycz, Michael W., Huang, Mia L., Kuzmenko, Ivan, Bu, Wei, Kirshenbaum, Kent, and Gidalevitz, David. Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes. United States: N. p., Web. doi:10.1016/j.bbamem.2018.03.021.
Andreev, Konstantin, Martynowycz, Michael W., Huang, Mia L., Kuzmenko, Ivan, Bu, Wei, Kirshenbaum, Kent, & Gidalevitz, David. Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes. United States. doi:10.1016/j.bbamem.2018.03.021.
Andreev, Konstantin, Martynowycz, Michael W., Huang, Mia L., Kuzmenko, Ivan, Bu, Wei, Kirshenbaum, Kent, and Gidalevitz, David. 2018. "Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes". United States. doi:10.1016/j.bbamem.2018.03.021. https://www.osti.gov/servlets/purl/1472076.
@article{osti_1472076,
title = {Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes},
author = {Andreev, Konstantin and Martynowycz, Michael W. and Huang, Mia L. and Kuzmenko, Ivan and Bu, Wei and Kirshenbaum, Kent and Gidalevitz, David},
abstractNote = {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, epi-fluorescence 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. In conclusion, it is suggested that peptoids may follow different optimization schemes as compared to their natural analogues.},
doi = {10.1016/j.bbamem.2018.03.021},
journal = {Biochimica et Biophysica Acta. Biomembranes},
number = 6,
volume = 1860,
place = {United States},
year = {2018},
month = {4}
}