The peptide antibiotic Clavanin A interacts strongly and specifically with lipid bilayers

E.J.M. van Kan; D.N. Ganchev; M.M.E. Snel; V. Chupin; A. van der Bent; B. de Kruijff

doi:10.1021/bi0349017

The peptide antibiotic Clavanin A interacts strongly and specifically with lipid bilayers

E.J.M. van Kan, D.N. Ganchev, M.M.E. Snel, V. Chupin, A. van der Bent, B. de Kruijff

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

39 Citations (Scopus)

Abstract

In this study the interaction of the antimicrobial peptide clavanin A with phosphatidylcholine bilayers is investigated by DSC, NMR, and AFM techniques. It is shown that the peptide interacts strongly and specifically with the lipids, resulting in increased order-disorder phase transition temperatures, phase separation, altered acyl chain and headgroup packing, and a drastically changed surface morphology of the bilayer. These results are interpreted in terms of clavanin-specific interactions with lipids and are discussed in the light of the different mechanisms by which clavanin A can destroy the barrier function of biological membranes

Original language	English
Pages (from-to)	11366-11372
Journal	Biochemistry
Volume	42
Issue number	38
DOIs	https://doi.org/10.1021/bi0349017
Publication status	Published - 2003

Keywords

helical antimicrobial peptides
nuclear-magnetic-resonance
differential scanning calorimetry
x-ray-diffraction
phosphatidylcholine bilayers
model membranes
transmembrane peptides
biological-membranes
tunicate hemocytes
flanking residues

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title = "The peptide antibiotic Clavanin A interacts strongly and specifically with lipid bilayers",

abstract = "In this study the interaction of the antimicrobial peptide clavanin A with phosphatidylcholine bilayers is investigated by DSC, NMR, and AFM techniques. It is shown that the peptide interacts strongly and specifically with the lipids, resulting in increased order-disorder phase transition temperatures, phase separation, altered acyl chain and headgroup packing, and a drastically changed surface morphology of the bilayer. These results are interpreted in terms of clavanin-specific interactions with lipids and are discussed in the light of the different mechanisms by which clavanin A can destroy the barrier function of biological membranes",

keywords = "helical antimicrobial peptides, nuclear-magnetic-resonance, differential scanning calorimetry, x-ray-diffraction, phosphatidylcholine bilayers, model membranes, transmembrane peptides, biological-membranes, tunicate hemocytes, flanking residues",

author = "\{van Kan\}, E.J.M. and D.N. Ganchev and M.M.E. Snel and V. Chupin and \{van der Bent\}, A. and \{de Kruijff\}, B.",

year = "2003",

doi = "10.1021/bi0349017",

language = "English",

volume = "42",

pages = "11366--11372",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society (ACS)",

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TY - JOUR

T1 - The peptide antibiotic Clavanin A interacts strongly and specifically with lipid bilayers

AU - van Kan, E.J.M.

AU - Ganchev, D.N.

AU - Snel, M.M.E.

AU - Chupin, V.

AU - van der Bent, A.

AU - de Kruijff, B.

PY - 2003

Y1 - 2003

N2 - In this study the interaction of the antimicrobial peptide clavanin A with phosphatidylcholine bilayers is investigated by DSC, NMR, and AFM techniques. It is shown that the peptide interacts strongly and specifically with the lipids, resulting in increased order-disorder phase transition temperatures, phase separation, altered acyl chain and headgroup packing, and a drastically changed surface morphology of the bilayer. These results are interpreted in terms of clavanin-specific interactions with lipids and are discussed in the light of the different mechanisms by which clavanin A can destroy the barrier function of biological membranes

AB - In this study the interaction of the antimicrobial peptide clavanin A with phosphatidylcholine bilayers is investigated by DSC, NMR, and AFM techniques. It is shown that the peptide interacts strongly and specifically with the lipids, resulting in increased order-disorder phase transition temperatures, phase separation, altered acyl chain and headgroup packing, and a drastically changed surface morphology of the bilayer. These results are interpreted in terms of clavanin-specific interactions with lipids and are discussed in the light of the different mechanisms by which clavanin A can destroy the barrier function of biological membranes

KW - helical antimicrobial peptides

KW - nuclear-magnetic-resonance

KW - differential scanning calorimetry

KW - x-ray-diffraction

KW - phosphatidylcholine bilayers

KW - model membranes

KW - transmembrane peptides

KW - biological-membranes

KW - tunicate hemocytes

KW - flanking residues

U2 - 10.1021/bi0349017

DO - 10.1021/bi0349017

M3 - Article

SN - 0006-2960

VL - 42

SP - 11366

EP - 11372

JO - Biochemistry

JF - Biochemistry

IS - 38

ER -

The peptide antibiotic Clavanin A interacts strongly and specifically with lipid bilayers

Abstract

Keywords

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