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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10.1016/j.bbamem.2018.03.021

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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 = "Publisher Copyright: {\textcopyright} 2018 Elsevier B.V.",

year = "2018",

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doi = "10.1016/j.bbamem.2018.03.021",

language = "English (US)",

volume = "1860",

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T1 - Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes

AU - Andreev, Konstantin

AU - Martynowycz, Michael W.

AU - Huang, Mia L.

AU - Kuzmenko, Ivan

AU - Bu, Wei

AU - Kirshenbaum, Kent

AU - Gidalevitz, David

PY - 2018/6

Y1 - 2018/6

N2 - 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.

AB - 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.

KW - AFM

KW - Antimicrobial peptoids

KW - Cytotoxicity

KW - Hydrophobicity

KW - Lipid membranes

KW - X-ray scattering

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SN - 0005-2736

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SP - 1414

EP - 1423

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

IS - 6

ER -

Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes

Abstract

Keywords

ASJC Scopus subject areas

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