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Communication : Alamethicin can capture lipid-like molecules in the membrane. / Afanasyeva, Ekaterina F.; Syryamina, Victoria N.; Dzuba, Sergei A.

In: Journal of Chemical Physics, Vol. 146, No. 1, 011103, 07.01.2017, p. 011103.

Research output: Contribution to journalArticlepeer-review

Harvard

Afanasyeva, EF, Syryamina, VN & Dzuba, SA 2017, 'Communication: Alamethicin can capture lipid-like molecules in the membrane', Journal of Chemical Physics, vol. 146, no. 1, 011103, pp. 011103. https://doi.org/10.1063/1.4973703

APA

Afanasyeva, E. F., Syryamina, V. N., & Dzuba, S. A. (2017). Communication: Alamethicin can capture lipid-like molecules in the membrane. Journal of Chemical Physics, 146(1), 011103. [011103]. https://doi.org/10.1063/1.4973703

Vancouver

Afanasyeva EF, Syryamina VN, Dzuba SA. Communication: Alamethicin can capture lipid-like molecules in the membrane. Journal of Chemical Physics. 2017 Jan 7;146(1):011103. 011103. doi: 10.1063/1.4973703

Author

Afanasyeva, Ekaterina F. ; Syryamina, Victoria N. ; Dzuba, Sergei A. / Communication : Alamethicin can capture lipid-like molecules in the membrane. In: Journal of Chemical Physics. 2017 ; Vol. 146, No. 1. pp. 011103.

BibTeX

@article{aac23cbe653d47a7b37aba27c360eff6,
title = "Communication: Alamethicin can capture lipid-like molecules in the membrane",
abstract = "Alamethicin (Alm) is a 19-mer antimicrobial peptide produced by fungus Trichoderma viride. Above a threshold concentration, Alm forms pores across the membrane, providing a mechanism of its antimicrobial action. Here we show that at a small concentration which is below the threshold value, Alm participates in formation of nanoscale lipid-mediated clusters of guest lipid-like molecules in the membrane. These results are obtained by electron spin echo (ESE) technique - a pulsed version of electron paramagnetic resonance - on spin-labeled stearic acid in a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayer with Alm added at 1/200 peptide-to-lipid ratio. ESE decay measurements are interpreted assuming that stearic acid molecules in the membrane are assembling around the Alm molecule. One may suggest that this Alm capturing effect on the guest lipid-like molecules could be important for the peptide antimicrobial action.",
keywords = "Alamethicin/chemistry, Amino Acid Sequence, Cell Membrane/drug effects, Electron Spin Resonance Spectroscopy, Phosphatidylcholines/chemistry, Temperature, CHOLESTEROL, MECHANISM, ANTIMICROBIAL PEPTIDES, BILAYER, DYNAMICS SIMULATIONS, RESONANCE, TEMPERATURE, ORIENTATION, MELITTIN, SPIN LABELS",
author = "Afanasyeva, {Ekaterina F.} and Syryamina, {Victoria N.} and Dzuba, {Sergei A.}",
year = "2017",
month = jan,
day = "7",
doi = "10.1063/1.4973703",
language = "English",
volume = "146",
pages = "011103",
journal = "Journal of Chemical Physics",
issn = "0021-9606",
publisher = "American Institute of Physics",
number = "1",

}

RIS

TY - JOUR

T1 - Communication

T2 - Alamethicin can capture lipid-like molecules in the membrane

AU - Afanasyeva, Ekaterina F.

AU - Syryamina, Victoria N.

AU - Dzuba, Sergei A.

PY - 2017/1/7

Y1 - 2017/1/7

N2 - Alamethicin (Alm) is a 19-mer antimicrobial peptide produced by fungus Trichoderma viride. Above a threshold concentration, Alm forms pores across the membrane, providing a mechanism of its antimicrobial action. Here we show that at a small concentration which is below the threshold value, Alm participates in formation of nanoscale lipid-mediated clusters of guest lipid-like molecules in the membrane. These results are obtained by electron spin echo (ESE) technique - a pulsed version of electron paramagnetic resonance - on spin-labeled stearic acid in a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayer with Alm added at 1/200 peptide-to-lipid ratio. ESE decay measurements are interpreted assuming that stearic acid molecules in the membrane are assembling around the Alm molecule. One may suggest that this Alm capturing effect on the guest lipid-like molecules could be important for the peptide antimicrobial action.

AB - Alamethicin (Alm) is a 19-mer antimicrobial peptide produced by fungus Trichoderma viride. Above a threshold concentration, Alm forms pores across the membrane, providing a mechanism of its antimicrobial action. Here we show that at a small concentration which is below the threshold value, Alm participates in formation of nanoscale lipid-mediated clusters of guest lipid-like molecules in the membrane. These results are obtained by electron spin echo (ESE) technique - a pulsed version of electron paramagnetic resonance - on spin-labeled stearic acid in a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayer with Alm added at 1/200 peptide-to-lipid ratio. ESE decay measurements are interpreted assuming that stearic acid molecules in the membrane are assembling around the Alm molecule. One may suggest that this Alm capturing effect on the guest lipid-like molecules could be important for the peptide antimicrobial action.

KW - Alamethicin/chemistry

KW - Amino Acid Sequence

KW - Cell Membrane/drug effects

KW - Electron Spin Resonance Spectroscopy

KW - Phosphatidylcholines/chemistry

KW - Temperature

KW - CHOLESTEROL

KW - MECHANISM

KW - ANTIMICROBIAL PEPTIDES

KW - BILAYER

KW - DYNAMICS SIMULATIONS

KW - RESONANCE

KW - TEMPERATURE

KW - ORIENTATION

KW - MELITTIN

KW - SPIN LABELS

UR - http://www.scopus.com/inward/record.url?scp=85009154231&partnerID=8YFLogxK

U2 - 10.1063/1.4973703

DO - 10.1063/1.4973703

M3 - Article

C2 - 28063425

AN - SCOPUS:85009154231

VL - 146

SP - 011103

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

SN - 0021-9606

IS - 1

M1 - 011103

ER -

ID: 10316640