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Interdisciplinary Nanoscience Center

Vladimir Matchkov

Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance

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Standard

Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance. / Hjørringgaard, Claudia Ulrich; Vad, Brian Stougaard; Matchkov, Vladimir et al.

In: Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, Vol. 116, No. 26, 05.07.2012, p. 7652-7659.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

MLA

Hjørringgaard, Claudia Ulrich et al. "Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance". Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical. 2012, 116(26). 7652-7659. https://doi.org/10.1021/jp2098679

Vancouver

Hjørringgaard CU, Vad BS, Matchkov V, Nielsen SB, Vosegaard T , Nielsen NC et al. Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance. Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical. 2012 Jul 5;116(26):7652-7659. doi: 10.1021/jp2098679

Author

Hjørringgaard, Claudia Ulrich ; Vad, Brian Stougaard ; Matchkov, Vladimir et al. / Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance. In: Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical. 2012 ; Vol. 116, No. 26. pp. 7652-7659.

Bibtex

@article{91ea127419e94e0096ea46f9b15931c5,

title = "Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance",

abstract = "Bacterial resistance to classical antibiotics is a serious medical problem, which continues to grow. Small antimicrobial peptides represent a potential solution and are increasingly being developed as novel therapeutic agents. Many of these peptides owe their antibacterial activity to the formation of trans-membrane ion-channels resulting in cell lysis. However, to further develop the field of peptide antibiotics, a thorough understanding of their mechanism of action is needed. Alamethicin belongs to a class of peptides called peptaibols and represents one of these antimicrobial peptides. To examine the dynamics of assembly and to facilitate a thorough structural evaluation of the alamethicin ion-channels, we have applied click chemistry for the synthesis of templated alamethicin multimers covalently attached to cyclodextrin-scaffolds. Using oriented circular dichroism, calcein release assays, and single-channel current measurements, the α-helices of the templated multimers were demonstrated to insert into lipid bilayers forming highly efficient and remarkably stable ion-channels",

author = "Hj{\o}rringgaard, {Claudia Ulrich} and Vad, {Brian Stougaard} and Vladimir Matchkov and Nielsen, {S{\o}ren Bang} and Thomas Vosegaard and Nielsen, {Niels Christian} and Daniel Otzen and Troels Skrydstrup",

year = "2012",

month = jul,

day = "5",

doi = "10.1021/jp2098679",

language = "English",

volume = "116",

pages = "7652--7659",

journal = "Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical",

issn = "1520-6106",

publisher = "American Chemical Society",

number = "26",

}

RIS

TY - JOUR

T1 - Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current Conductance

AU - Hjørringgaard, Claudia Ulrich

AU - Vad, Brian Stougaard

AU - Matchkov, Vladimir

AU - Nielsen, Søren Bang

AU - Vosegaard, Thomas

AU - Nielsen, Niels Christian

AU - Otzen, Daniel

AU - Skrydstrup, Troels

PY - 2012/7/5

Y1 - 2012/7/5

N2 - Bacterial resistance to classical antibiotics is a serious medical problem, which continues to grow. Small antimicrobial peptides represent a potential solution and are increasingly being developed as novel therapeutic agents. Many of these peptides owe their antibacterial activity to the formation of trans-membrane ion-channels resulting in cell lysis. However, to further develop the field of peptide antibiotics, a thorough understanding of their mechanism of action is needed. Alamethicin belongs to a class of peptides called peptaibols and represents one of these antimicrobial peptides. To examine the dynamics of assembly and to facilitate a thorough structural evaluation of the alamethicin ion-channels, we have applied click chemistry for the synthesis of templated alamethicin multimers covalently attached to cyclodextrin-scaffolds. Using oriented circular dichroism, calcein release assays, and single-channel current measurements, the α-helices of the templated multimers were demonstrated to insert into lipid bilayers forming highly efficient and remarkably stable ion-channels

AB - Bacterial resistance to classical antibiotics is a serious medical problem, which continues to grow. Small antimicrobial peptides represent a potential solution and are increasingly being developed as novel therapeutic agents. Many of these peptides owe their antibacterial activity to the formation of trans-membrane ion-channels resulting in cell lysis. However, to further develop the field of peptide antibiotics, a thorough understanding of their mechanism of action is needed. Alamethicin belongs to a class of peptides called peptaibols and represents one of these antimicrobial peptides. To examine the dynamics of assembly and to facilitate a thorough structural evaluation of the alamethicin ion-channels, we have applied click chemistry for the synthesis of templated alamethicin multimers covalently attached to cyclodextrin-scaffolds. Using oriented circular dichroism, calcein release assays, and single-channel current measurements, the α-helices of the templated multimers were demonstrated to insert into lipid bilayers forming highly efficient and remarkably stable ion-channels

U2 - 10.1021/jp2098679

DO - 10.1021/jp2098679

M3 - Journal article

C2 - 22676384

VL - 116

SP - 7652

EP - 7659

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 - 26

ER -