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IN VITRO INTERACTION OF THE AEDL PEPTIDE WITH DNA. / Morozova, E. A.; Kasyanenko, N. A.; Lin'kova, N. S.; Khavinson, V. Kh.; Soloviev, A. Yu.

In: Journal of Structural Chemistry, Vol. 58, No. 2, 03.2017, p. 420-424.

Research output: Contribution to journal › Article › peer-review

Harvard

Morozova, EA, Kasyanenko, NA, Lin'kova, NS, Khavinson, VK & Soloviev, AY 2017, 'IN VITRO INTERACTION OF THE AEDL PEPTIDE WITH DNA', Journal of Structural Chemistry, vol. 58, no. 2, pp. 420-424. https://doi.org/10.1134/S0022476617020299

APA

Morozova, E. A., Kasyanenko, N. A., Lin'kova, N. S., Khavinson, V. K., & Soloviev, A. Y. (2017). IN VITRO INTERACTION OF THE AEDL PEPTIDE WITH DNA. Journal of Structural Chemistry, 58(2), 420-424. https://doi.org/10.1134/S0022476617020299

Vancouver

Morozova EA, Kasyanenko NA, Lin'kova NS, Khavinson VK, Soloviev AY. IN VITRO INTERACTION OF THE AEDL PEPTIDE WITH DNA. Journal of Structural Chemistry. 2017 Mar;58(2):420-424. https://doi.org/10.1134/S0022476617020299

Author

Morozova, E. A. ; Kasyanenko, N. A. ; Lin'kova, N. S. ; Khavinson, V. Kh. ; Soloviev, A. Yu. / IN VITRO INTERACTION OF THE AEDL PEPTIDE WITH DNA. In: Journal of Structural Chemistry. 2017 ; Vol. 58, No. 2. pp. 420-424.

BibTeX

@article{d81f3ef2eb0b4b2b8dc8a29d3b679cc4,
title = "IN VITRO INTERACTION OF THE AEDL PEPTIDE WITH DNA",
abstract = "In the cell culture experiments, the AEDL peptide proved to be an efficient agent stimulating the cell renewal processes and the enhancement of the functional activity of bronchial epithelial cells. A presumed target of the peptide action is a DNA molecule. The work studies the peptide binding with high-molecular DNA in solutions with different ionic strengths. The spectral (UV spectophotometery and circular dichroism) and hydrodynamic (viscosimetry) methods show that, under the experimental conditions, the AEDL peptide forms a complex with DNA and that nitrogen bases are involved in the binding. The character of spectral changes in DNA suggests a possible interaction of the AEDL peptide with DNA in the major furrow at the guanine N7 site without a visible distortion of the double helix structure.",
keywords = "AEDL tetrapeptide, bronchial epithelium, DNA-peptide interactions, circular dichroism, viscosimetry",
author = "Morozova, {E. A.} and Kasyanenko, {N. A.} and Lin'kova, {N. S.} and Khavinson, {V. Kh.} and Soloviev, {A. Yu.}",
year = "2017",
month = mar,
doi = "10.1134/S0022476617020299",
language = "Английский",
volume = "58",
pages = "420--424",
journal = "Journal of Structural Chemistry",
issn = "0022-4766",
publisher = "Springer Nature",
number = "2",
note = "null ; Conference date: 23-06-2014 Through 27-06-2014",

}

RIS

TY - JOUR

T1 - IN VITRO INTERACTION OF THE AEDL PEPTIDE WITH DNA

AU - Morozova, E. A.

AU - Kasyanenko, N. A.

AU - Lin'kova, N. S.

AU - Khavinson, V. Kh.

AU - Soloviev, A. Yu.

PY - 2017/3

Y1 - 2017/3

N2 - In the cell culture experiments, the AEDL peptide proved to be an efficient agent stimulating the cell renewal processes and the enhancement of the functional activity of bronchial epithelial cells. A presumed target of the peptide action is a DNA molecule. The work studies the peptide binding with high-molecular DNA in solutions with different ionic strengths. The spectral (UV spectophotometery and circular dichroism) and hydrodynamic (viscosimetry) methods show that, under the experimental conditions, the AEDL peptide forms a complex with DNA and that nitrogen bases are involved in the binding. The character of spectral changes in DNA suggests a possible interaction of the AEDL peptide with DNA in the major furrow at the guanine N7 site without a visible distortion of the double helix structure.

AB - In the cell culture experiments, the AEDL peptide proved to be an efficient agent stimulating the cell renewal processes and the enhancement of the functional activity of bronchial epithelial cells. A presumed target of the peptide action is a DNA molecule. The work studies the peptide binding with high-molecular DNA in solutions with different ionic strengths. The spectral (UV spectophotometery and circular dichroism) and hydrodynamic (viscosimetry) methods show that, under the experimental conditions, the AEDL peptide forms a complex with DNA and that nitrogen bases are involved in the binding. The character of spectral changes in DNA suggests a possible interaction of the AEDL peptide with DNA in the major furrow at the guanine N7 site without a visible distortion of the double helix structure.

KW - AEDL tetrapeptide

KW - bronchial epithelium

KW - DNA-peptide interactions

KW - circular dichroism

KW - viscosimetry

U2 - 10.1134/S0022476617020299

DO - 10.1134/S0022476617020299

M3 - статья

VL - 58

SP - 420

EP - 424

JO - Journal of Structural Chemistry

JF - Journal of Structural Chemistry

SN - 0022-4766

IS - 2

Y2 - 23 June 2014 through 27 June 2014

ER -

ID: 73398260