Impact of the antimicrobial peptide Novicidin on membrane structure and integrity

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Impact of the antimicrobial peptide Novicidin on membrane structure and integrity. / Nielsen, Søren B; Otzen, Daniel Erik.

I: Journal of Colloid and Interface Science, Bind 345, Nr. 2, 28.01.2010, s. 248-256.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Nielsen, SB & Otzen, DE 2010, 'Impact of the antimicrobial peptide Novicidin on membrane structure and integrity', Journal of Colloid and Interface Science, bind 345, nr. 2, s. 248-256. https://doi.org/10.1016/j.jcis.2010.01.065

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Nielsen, Søren B ; Otzen, Daniel Erik. / Impact of the antimicrobial peptide Novicidin on membrane structure and integrity. I: Journal of Colloid and Interface Science. 2010 ; Bind 345, Nr. 2. s. 248-256.

Bibtex

@article{f00881b05db411df8b17000ea68e967b,
title = "Impact of the antimicrobial peptide Novicidin on membrane structure and integrity",
abstract = "We have studied the impact of an 18-residue cationic antimicrobial peptide Novicidin (Nc) on the structure and integrity of partially anionic lipid membranes using oriented circular dichroism (OCD), quartz crystal microbalance with dissipation (QCM-D), dual polarization interferometry (DPI), calcein dye leakage and fluorescence spectroscopy. OCD consistently showed that Nc is bound in an alpha-helical, surface bound state over a range of peptide to lipid (P/L) ratios up to approximately 1:15. Realignment of Nc at higher P/L ratios correlates to loss of membrane integrity as shown by Laurdan fluorescence spectroscopy and by loss of lipid alignment in DPI analysis. Laurdan generalized polarity shows a decrease in water accessibility or mobility in the hydrophobic/hydrophilic interface of the lipid membrane, consistent with rearrangement of lipid packing. QCM-D studies on the interaction of Nc with lipid membranes emphasize the importance of including the dissipation factor in data analysis, revealing formation of a highly hydrated film after exposure to 3muMNc. Our findings suggest a carpet mechanism of membrane disruption in which peptide binding first induces leakage at a critical surface concentration, probably through formation of transient pores or transient disruption of the membrane integrity, followed by more extensive membrane disintegration at higher P/L ratios.",
author = "Nielsen, {S{\o}ren B} and Otzen, {Daniel Erik}",
note = "Copyright {\circledC} 2010 Elsevier Inc. All rights reserved.",
year = "2010",
month = "1",
day = "28",
doi = "10.1016/j.jcis.2010.01.065",
language = "English",
volume = "345",
pages = "248--256",
journal = "Journal of Colloid and Interface Science",
issn = "0021-9797",
publisher = "Academic Press",
number = "2",

}

RIS

TY - JOUR

T1 - Impact of the antimicrobial peptide Novicidin on membrane structure and integrity

AU - Nielsen, Søren B

AU - Otzen, Daniel Erik

N1 - Copyright © 2010 Elsevier Inc. All rights reserved.

PY - 2010/1/28

Y1 - 2010/1/28

N2 - We have studied the impact of an 18-residue cationic antimicrobial peptide Novicidin (Nc) on the structure and integrity of partially anionic lipid membranes using oriented circular dichroism (OCD), quartz crystal microbalance with dissipation (QCM-D), dual polarization interferometry (DPI), calcein dye leakage and fluorescence spectroscopy. OCD consistently showed that Nc is bound in an alpha-helical, surface bound state over a range of peptide to lipid (P/L) ratios up to approximately 1:15. Realignment of Nc at higher P/L ratios correlates to loss of membrane integrity as shown by Laurdan fluorescence spectroscopy and by loss of lipid alignment in DPI analysis. Laurdan generalized polarity shows a decrease in water accessibility or mobility in the hydrophobic/hydrophilic interface of the lipid membrane, consistent with rearrangement of lipid packing. QCM-D studies on the interaction of Nc with lipid membranes emphasize the importance of including the dissipation factor in data analysis, revealing formation of a highly hydrated film after exposure to 3muMNc. Our findings suggest a carpet mechanism of membrane disruption in which peptide binding first induces leakage at a critical surface concentration, probably through formation of transient pores or transient disruption of the membrane integrity, followed by more extensive membrane disintegration at higher P/L ratios.

AB - We have studied the impact of an 18-residue cationic antimicrobial peptide Novicidin (Nc) on the structure and integrity of partially anionic lipid membranes using oriented circular dichroism (OCD), quartz crystal microbalance with dissipation (QCM-D), dual polarization interferometry (DPI), calcein dye leakage and fluorescence spectroscopy. OCD consistently showed that Nc is bound in an alpha-helical, surface bound state over a range of peptide to lipid (P/L) ratios up to approximately 1:15. Realignment of Nc at higher P/L ratios correlates to loss of membrane integrity as shown by Laurdan fluorescence spectroscopy and by loss of lipid alignment in DPI analysis. Laurdan generalized polarity shows a decrease in water accessibility or mobility in the hydrophobic/hydrophilic interface of the lipid membrane, consistent with rearrangement of lipid packing. QCM-D studies on the interaction of Nc with lipid membranes emphasize the importance of including the dissipation factor in data analysis, revealing formation of a highly hydrated film after exposure to 3muMNc. Our findings suggest a carpet mechanism of membrane disruption in which peptide binding first induces leakage at a critical surface concentration, probably through formation of transient pores or transient disruption of the membrane integrity, followed by more extensive membrane disintegration at higher P/L ratios.

U2 - 10.1016/j.jcis.2010.01.065

DO - 10.1016/j.jcis.2010.01.065

M3 - Journal article

C2 - 20153477

VL - 345

SP - 248

EP - 256

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

SN - 0021-9797

IS - 2

ER -