Research output: Contribution to journal › Article › peer-review
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.
In: Journal of Photochemistry and Photobiology A: Chemistry, Vol. 354, 2018, p. 86-100.Research output: Contribution to journal › Article › peer-review
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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