Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides

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Standard

Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR : altered structural information in studies of antimicrobial peptides. / Bertelsen, Kresten; Vad, Brian; Nielsen, Erik Holm Toustrup; Hansen, Sara K; Skrydstrup, Troels; Otzen, Daniel; Vosegaard, Thomas; Nielsen, Niels Christian.

In: Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, Vol. 115, No. 8, 2011, p. 1767-1774.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Bertelsen, K, Vad, B, Nielsen, EHT, Hansen, SK, Skrydstrup, T, Otzen, D, Vosegaard, T & Nielsen, NC 2011, 'Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides', Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, vol. 115, no. 8, pp. 1767-1774. https://doi.org/10.1021/jp110866g

APA

Bertelsen, K., Vad, B., Nielsen, E. H. T., Hansen, S. K., Skrydstrup, T., Otzen, D., ... Nielsen, N. C. (2011). Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, 115(8), 1767-1774. https://doi.org/10.1021/jp110866g

CBE

MLA

Bertelsen, Kresten et al. "Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides". Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical. 2011, 115(8). 1767-1774. https://doi.org/10.1021/jp110866g

Vancouver

Bertelsen K, Vad B, Nielsen EHT, Hansen SK, Skrydstrup T, Otzen D et al. Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical. 2011;115(8):1767-1774. https://doi.org/10.1021/jp110866g

Author

Bertelsen, Kresten ; Vad, Brian ; Nielsen, Erik Holm Toustrup ; Hansen, Sara K ; Skrydstrup, Troels ; Otzen, Daniel ; Vosegaard, Thomas ; Nielsen, Niels Christian. / Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR : altered structural information in studies of antimicrobial peptides. In: Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical. 2011 ; Vol. 115, No. 8. pp. 1767-1774.

Bibtex

@article{3c6f687725934fc396f6fd1ad6e38319,
title = "Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides",
abstract = "Recently, ether lipids have been introduced as long-term stable alternatives to the more natural, albeit easier degradable, ester lipids in the preparation of oriented lipid bilayers and bicelles for oriented-sample solid-state NMR spectroscopy. Here we report that ether lipids such as the frequently used 14-O-PC (1,2-di-O-tetradecyl-sn-glycero-3-phosphocholine) may induce significant changes in the structure and dynamics, including altered interaction between peptides and lipids relative to what is observed with the more conventionally used DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) bilayers. Such effects are demonstrated for the antimicrobial peptide novicidin, for which 2D separate-local-field NMR and circular dichroism experiments reveal significant structural/conformational differences for the peptide in the two different lipid systems. Likewise, we observe altered secondary structure and different temperature-dependent membrane anchoring for the antimicrobial peptide alamethicin depending on whether the peptide is reconstituted into ester or ether lipids. Such observations are not particularly surprising considering the significant difference of the lipids in the phosphorus headgroup and they may provide important new insight into the delicate peptide-membrane interactions in the systems studied. In contrast, these observations reinforce the need to carefully consider potential structural changes in addition to long-term stability prior to the selection of membrane environment of membrane proteins in the analysis of their structure and dynamics. In more general terms, the results underscore the necessity in structural biology to address both the protein and its environments in studies relating structure to function.",
keywords = "Antimicrobial Cationic Peptides, Circular Dichroism, Dimyristoylphosphatidylcholine, Lipid Bilayers, Magnetic Resonance Spectroscopy, Phospholipid Ethers",
author = "Kresten Bertelsen and Brian Vad and Nielsen, {Erik Holm Toustrup} and Hansen, {Sara K} and Troels Skrydstrup and Daniel Otzen and Thomas Vosegaard and Nielsen, {Niels Christian}",
note = "{\circledC} 2011 American Chemical Society",
year = "2011",
doi = "10.1021/jp110866g",
language = "English",
volume = "115",
pages = "1767--1774",
journal = "Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "8",

}

RIS

TY - JOUR

T1 - Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR

T2 - altered structural information in studies of antimicrobial peptides

AU - Bertelsen, Kresten

AU - Vad, Brian

AU - Nielsen, Erik Holm Toustrup

AU - Hansen, Sara K

AU - Skrydstrup, Troels

AU - Otzen, Daniel

AU - Vosegaard, Thomas

AU - Nielsen, Niels Christian

N1 - © 2011 American Chemical Society

PY - 2011

Y1 - 2011

N2 - Recently, ether lipids have been introduced as long-term stable alternatives to the more natural, albeit easier degradable, ester lipids in the preparation of oriented lipid bilayers and bicelles for oriented-sample solid-state NMR spectroscopy. Here we report that ether lipids such as the frequently used 14-O-PC (1,2-di-O-tetradecyl-sn-glycero-3-phosphocholine) may induce significant changes in the structure and dynamics, including altered interaction between peptides and lipids relative to what is observed with the more conventionally used DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) bilayers. Such effects are demonstrated for the antimicrobial peptide novicidin, for which 2D separate-local-field NMR and circular dichroism experiments reveal significant structural/conformational differences for the peptide in the two different lipid systems. Likewise, we observe altered secondary structure and different temperature-dependent membrane anchoring for the antimicrobial peptide alamethicin depending on whether the peptide is reconstituted into ester or ether lipids. Such observations are not particularly surprising considering the significant difference of the lipids in the phosphorus headgroup and they may provide important new insight into the delicate peptide-membrane interactions in the systems studied. In contrast, these observations reinforce the need to carefully consider potential structural changes in addition to long-term stability prior to the selection of membrane environment of membrane proteins in the analysis of their structure and dynamics. In more general terms, the results underscore the necessity in structural biology to address both the protein and its environments in studies relating structure to function.

AB - Recently, ether lipids have been introduced as long-term stable alternatives to the more natural, albeit easier degradable, ester lipids in the preparation of oriented lipid bilayers and bicelles for oriented-sample solid-state NMR spectroscopy. Here we report that ether lipids such as the frequently used 14-O-PC (1,2-di-O-tetradecyl-sn-glycero-3-phosphocholine) may induce significant changes in the structure and dynamics, including altered interaction between peptides and lipids relative to what is observed with the more conventionally used DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) bilayers. Such effects are demonstrated for the antimicrobial peptide novicidin, for which 2D separate-local-field NMR and circular dichroism experiments reveal significant structural/conformational differences for the peptide in the two different lipid systems. Likewise, we observe altered secondary structure and different temperature-dependent membrane anchoring for the antimicrobial peptide alamethicin depending on whether the peptide is reconstituted into ester or ether lipids. Such observations are not particularly surprising considering the significant difference of the lipids in the phosphorus headgroup and they may provide important new insight into the delicate peptide-membrane interactions in the systems studied. In contrast, these observations reinforce the need to carefully consider potential structural changes in addition to long-term stability prior to the selection of membrane environment of membrane proteins in the analysis of their structure and dynamics. In more general terms, the results underscore the necessity in structural biology to address both the protein and its environments in studies relating structure to function.

KW - Antimicrobial Cationic Peptides

KW - Circular Dichroism

KW - Dimyristoylphosphatidylcholine

KW - Lipid Bilayers

KW - Magnetic Resonance Spectroscopy

KW - Phospholipid Ethers

U2 - 10.1021/jp110866g

DO - 10.1021/jp110866g

M3 - Journal article

C2 - 21309516

VL - 115

SP - 1767

EP - 1774

JO - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

JF - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

SN - 1520-6106

IS - 8

ER -