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

doi:10.1016/j.bbamem.2018.03.021

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

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

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 language	English (US)
Pages (from-to)	1414-1423
Number of pages	10
Journal	Biochimica et Biophysica Acta - Biomembranes
Volume	1860
Issue number	6
DOIs	https://doi.org/10.1016/j.bbamem.2018.03.021
State	Published - Jun 2018

Keywords

AFM
Antimicrobial peptoids
Cytotoxicity
Hydrophobicity
Lipid membranes
X-ray scattering

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

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Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes. / Andreev, Konstantin; Martynowycz, Michael W.; Huang, Mia L.; Kuzmenko, Ivan; Bu, Wei; Kirshenbaum, Kent; Gidalevitz, David.

In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1860, No. 6, 06.2018, p. 1414-1423.

Research output: Contribution to journal › Article › peer-review

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title = "Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes",

abstract = "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.",

keywords = "AFM, Antimicrobial peptoids, Cytotoxicity, Hydrophobicity, Lipid membranes, X-ray scattering",

author = "Konstantin Andreev and Martynowycz, {Michael W.} and Huang, {Mia L.} and Ivan Kuzmenko and Wei Bu and Kent Kirshenbaum and David Gidalevitz",

note = "Funding Information: This research was supported by the NIH ( R01 AI073892 , D.G.), NSF ( CHE-1507946 , K.K.) and DARPA ( W911NF-09-1-378 D.G.). ChemMatCARS Sector 15 is supported by the National Science Foundation under grant number NSF/CHE-1346572 . This research used resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. M. W. Martynowycz was partially supported by the NSF via a fellowship through the Adler Planetary & Astronomy Museum, the laboratory-graduate fellowship at Argonne National Laboratory, and the Dean's fellowship at the Illinois Institute of Technology.",

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AU - Bu, Wei

AU - Kirshenbaum, Kent

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