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Insight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation. / Pomogaev, Vladimir A.; Ramazanov, Ruslan R.; Ruud, Kenneth; Artyukhov, Victor Ya.

в: Journal of Photochemistry and Photobiology A: Chemistry, Том 354, 2018, стр. 86-100.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Pomogaev, VA, Ramazanov, RR, Ruud, K & Artyukhov, VY 2018, 'Insight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation', Journal of Photochemistry and Photobiology A: Chemistry, Том. 354, стр. 86-100. https://doi.org/10.1016/j.jphotochem.2017.08.041

APA

Pomogaev, V. A., Ramazanov, R. R., Ruud, K., & Artyukhov, V. Y. (2018). Insight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation. Journal of Photochemistry and Photobiology A: Chemistry, 354, 86-100. https://doi.org/10.1016/j.jphotochem.2017.08.041

Vancouver

Pomogaev VA, Ramazanov RR, Ruud K, Artyukhov VY. Insight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation. Journal of Photochemistry and Photobiology A: Chemistry. 2018;354:86-100. https://doi.org/10.1016/j.jphotochem.2017.08.041

Author

Pomogaev, Vladimir A. ; Ramazanov, Ruslan R. ; Ruud, Kenneth ; Artyukhov, Victor Ya. / Insight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation. в: Journal of Photochemistry and Photobiology A: Chemistry. 2018 ; Том 354. стр. 86-100.

BibTeX

@article{829817ebcffc4a27b9bf50414d64b643,
title = "Insight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation",
abstract = "Spectroscopy is an important tool for detecting drug binding to amino acid sequences. One such important spectroscopic process is the fluorescence quenching due to charge transfer (CT) processes between a drug molecule and the chromophore center of Human Serum Albumin (HSA). We present a theoretical investigation of the CT occurring upon electronic excitation when a dimetridazole (Dmz) molecule incorporated in HSA interacts with tryptophan residue (Trp214). Structures of the donor–acceptor complexes were optimized using density-functional theory in vacuum as well as extracted from molecular dynamics (MD) trajectories of the Dmz and Trp214 complexes in HSA (Dmz&Trp214@HSA). Absorption, emission, and fluorescence quenching of the Trp214&Dmz complex in a large number of MD conformers were calculated using various quantum-mechanical approaches in order to generate statistical spectra that are then used for studying the CT between the non-bonded donor and the acceptor.",
keywords = "Human serum albumin, Tryptophan residue, Dimetridazole acceptor, Molecular dynamics, Quantum-mechanics, Charge transfer, Human serum albumin, Tryptophan residue, Dimetridazole acceptor, Molecular dynamics, Quantum-mechanics, Charge transfer",
author = "Pomogaev, {Vladimir A.} and Ramazanov, {Ruslan R.} and Kenneth Ruud and Artyukhov, {Victor Ya.}",
year = "2018",
doi = "10.1016/j.jphotochem.2017.08.041",
language = "English",
volume = "354",
pages = "86--100",
journal = "Journal of Photochemistry and Photobiology A: Chemistry",
issn = "1010-6030",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Insight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation

AU - Pomogaev, Vladimir A.

AU - Ramazanov, Ruslan R.

AU - Ruud, Kenneth

AU - Artyukhov, Victor Ya.

PY - 2018

Y1 - 2018

N2 - Spectroscopy is an important tool for detecting drug binding to amino acid sequences. One such important spectroscopic process is the fluorescence quenching due to charge transfer (CT) processes between a drug molecule and the chromophore center of Human Serum Albumin (HSA). We present a theoretical investigation of the CT occurring upon electronic excitation when a dimetridazole (Dmz) molecule incorporated in HSA interacts with tryptophan residue (Trp214). Structures of the donor–acceptor complexes were optimized using density-functional theory in vacuum as well as extracted from molecular dynamics (MD) trajectories of the Dmz and Trp214 complexes in HSA (Dmz&Trp214@HSA). Absorption, emission, and fluorescence quenching of the Trp214&Dmz complex in a large number of MD conformers were calculated using various quantum-mechanical approaches in order to generate statistical spectra that are then used for studying the CT between the non-bonded donor and the acceptor.

AB - Spectroscopy is an important tool for detecting drug binding to amino acid sequences. One such important spectroscopic process is the fluorescence quenching due to charge transfer (CT) processes between a drug molecule and the chromophore center of Human Serum Albumin (HSA). We present a theoretical investigation of the CT occurring upon electronic excitation when a dimetridazole (Dmz) molecule incorporated in HSA interacts with tryptophan residue (Trp214). Structures of the donor–acceptor complexes were optimized using density-functional theory in vacuum as well as extracted from molecular dynamics (MD) trajectories of the Dmz and Trp214 complexes in HSA (Dmz&Trp214@HSA). Absorption, emission, and fluorescence quenching of the Trp214&Dmz complex in a large number of MD conformers were calculated using various quantum-mechanical approaches in order to generate statistical spectra that are then used for studying the CT between the non-bonded donor and the acceptor.

KW - Human serum albumin

KW - Tryptophan residue

KW - Dimetridazole acceptor

KW - Molecular dynamics

KW - Quantum-mechanics

KW - Charge transfer

KW - Human serum albumin

KW - Tryptophan residue

KW - Dimetridazole acceptor

KW - Molecular dynamics

KW - Quantum-mechanics

KW - Charge transfer

U2 - 10.1016/j.jphotochem.2017.08.041

DO - 10.1016/j.jphotochem.2017.08.041

M3 - Article

VL - 354

SP - 86

EP - 100

JO - Journal of Photochemistry and Photobiology A: Chemistry

JF - Journal of Photochemistry and Photobiology A: Chemistry

SN - 1010-6030

ER -

ID: 9906142