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Eurocin, a new fungal defensin: structure, lipid binding and its mode of action

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Eurocin, a new fungal defensin: structure, lipid binding and its mode of action. / Oeemig, Jesper S; Lynggaard, Carina; Knudsen, Daniel et al.
In: Journal of Biological Chemistry, Vol. 7, 07.12.2012, p. 42361-42372.

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

Harvard

Oeemig, JS, Lynggaard, C, Knudsen, D, Hansen, FT, Noergaard, KD, Schneider, T, Vad, BS, Sandvang, D, Nielsen, L, Neve, S, Kristensen, H-H, Sahl, H-G, Otzen, D & Wimmer, R 2012, 'Eurocin, a new fungal defensin: structure, lipid binding and its mode of action', Journal of Biological Chemistry, vol. 7, pp. 42361-42372. https://doi.org/10.1074/jbc.M112.382028

APA

Oeemig, J. S., Lynggaard, C., Knudsen, D., Hansen, F. T., Noergaard, K. D., Schneider, T., Vad, B. S., Sandvang, D., Nielsen, L., Neve, S., Kristensen, H-H., Sahl, H-G., Otzen, D., & Wimmer, R. (2012). Eurocin, a new fungal defensin: structure, lipid binding and its mode of action. Journal of Biological Chemistry, 7, 42361-42372. https://doi.org/10.1074/jbc.M112.382028

CBE

Oeemig JS, Lynggaard C, Knudsen D, Hansen FT, Noergaard KD, Schneider T, Vad BS, Sandvang D, Nielsen L, Neve S, et al. 2012. Eurocin, a new fungal defensin: structure, lipid binding and its mode of action. Journal of Biological Chemistry. 7:42361-42372. https://doi.org/10.1074/jbc.M112.382028

MLA

Oeemig, Jesper S et al. "Eurocin, a new fungal defensin: structure, lipid binding and its mode of action". Journal of Biological Chemistry. 2012, 7. 42361-42372. https://doi.org/10.1074/jbc.M112.382028

Vancouver

Oeemig JS, Lynggaard C, Knudsen D, Hansen FT, Noergaard KD, Schneider T et al. Eurocin, a new fungal defensin: structure, lipid binding and its mode of action. Journal of Biological Chemistry. 2012 Dec 7;7:42361-42372. doi: 10.1074/jbc.M112.382028

Author

Oeemig, Jesper S ; Lynggaard, Carina ; Knudsen, Daniel et al. / Eurocin, a new fungal defensin : structure, lipid binding and its mode of action. In: Journal of Biological Chemistry. 2012 ; Vol. 7. pp. 42361-42372.

Bibtex

@article{da7844f6523d4a539402505cd66c521a,
title = "Eurocin, a new fungal defensin: structure, lipid binding and its mode of action",
abstract = "Antimicrobial peptides are a new class of antibiotics that are promising for pharmaceutical applications, since they have retained efficacy throughout evolution. One class of antimicrobial peptides are the defensins, that have been found in different species. Here we describe a new fungal defensin, eurocin. Eurocin acts against a range of gram-positive human pathogens, but not against gram-negative bacteria. Eurocin consists of 42 amino acids, forming a cysteine-stabilized α/β fold. Thermal denaturation data point shows the disulphide bridges being responsible for the stability of the fold. Eurocin does not form pores in cell membranes at physiologically relevant concentrations, it does, however, lead to limited leakage of a fluorophore from small unilamellar vesicles. Eurocin interacts with detergent micelles, and it inhibits the synthesis of cell walls by binding equimolarly to the cell wall precursor lipid II.",
author = "Oeemig, {Jesper S} and Carina Lynggaard and Daniel Knudsen and Hansen, {Frederik T} and Noergaard, {Kent D} and Tanja Schneider and Vad, {Brian S} and Dorthe Sandvang and Line Nielsen and Soeren Neve and Hans-Henrik Kristensen and Hans-Georg Sahl and Daniel Otzen and Reinhard Wimmer",
year = "2012",
month = dec,
day = "7",
doi = "10.1074/jbc.M112.382028",
language = "English",
volume = "7",
pages = "42361--42372",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

}

RIS

TY - JOUR

T1 - Eurocin, a new fungal defensin

T2 - structure, lipid binding and its mode of action

AU - Oeemig, Jesper S

AU - Lynggaard, Carina

AU - Knudsen, Daniel

AU - Hansen, Frederik T

AU - Noergaard, Kent D

AU - Schneider, Tanja

AU - Vad, Brian S

AU - Sandvang, Dorthe

AU - Nielsen, Line

AU - Neve, Soeren

AU - Kristensen, Hans-Henrik

AU - Sahl, Hans-Georg

AU - Otzen, Daniel

AU - Wimmer, Reinhard

PY - 2012/12/7

Y1 - 2012/12/7

N2 - Antimicrobial peptides are a new class of antibiotics that are promising for pharmaceutical applications, since they have retained efficacy throughout evolution. One class of antimicrobial peptides are the defensins, that have been found in different species. Here we describe a new fungal defensin, eurocin. Eurocin acts against a range of gram-positive human pathogens, but not against gram-negative bacteria. Eurocin consists of 42 amino acids, forming a cysteine-stabilized α/β fold. Thermal denaturation data point shows the disulphide bridges being responsible for the stability of the fold. Eurocin does not form pores in cell membranes at physiologically relevant concentrations, it does, however, lead to limited leakage of a fluorophore from small unilamellar vesicles. Eurocin interacts with detergent micelles, and it inhibits the synthesis of cell walls by binding equimolarly to the cell wall precursor lipid II.

AB - Antimicrobial peptides are a new class of antibiotics that are promising for pharmaceutical applications, since they have retained efficacy throughout evolution. One class of antimicrobial peptides are the defensins, that have been found in different species. Here we describe a new fungal defensin, eurocin. Eurocin acts against a range of gram-positive human pathogens, but not against gram-negative bacteria. Eurocin consists of 42 amino acids, forming a cysteine-stabilized α/β fold. Thermal denaturation data point shows the disulphide bridges being responsible for the stability of the fold. Eurocin does not form pores in cell membranes at physiologically relevant concentrations, it does, however, lead to limited leakage of a fluorophore from small unilamellar vesicles. Eurocin interacts with detergent micelles, and it inhibits the synthesis of cell walls by binding equimolarly to the cell wall precursor lipid II.

U2 - 10.1074/jbc.M112.382028

DO - 10.1074/jbc.M112.382028

M3 - Journal article

C2 - 23093408

VL - 7

SP - 42361

EP - 42372

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -