Ferrihydrite nanoparticles insights: Structural characterization, lactate dehydrogenase binding and virtual screening assay | Научно-инновационный портал СФУ

Ferrihydrite nanoparticles insights: Structural characterization, lactate dehydrogenase binding and virtual screening assay

Тип публикации: статья из журнала

Год издания: 2020

Идентификатор DOI: 10.1016/j.ijbiomac.2020.08.242

Ключевые слова: binding mechanism, energy transfer, ferrihydrite nanoparticles, lactate dehydrogenase, thermodynamic fingerprint, virtual screeningthe work was accomplished in the frame of jinr themes 02-1-1107-2011/2021, 04-5-1131-2017/2021 and 04-4-1121-2015/2020 and with the financial support of the ro-jinr projects nos. 268/21.05.2020 items 8 and 77, and 269/21.05.2020 items 11 and – 80. mb acknowledges dr. alexander kuklin for assistance for sans measurements and fruitful discussions. the authors acknowledge dr. george stan of the national institute of materials physics for facilitating the conduct of ftir experiments.

Аннотация: The binding between the enzyme lactate dehydrogenase (LDH) and ferrihydrite nanoparticles (Fh-NPs) was investigated by means of small-angle neutron scattering (SANS), Fourier-transform infrared (FTIR) spectroscopy, fluorescence and Förster resonance energy transfer (FRET) and molecular docking. Fh-NPs - LDH compounds of dimensions under 100 nm are formed. The conformational changes and the mechanism of interaction between LDH and Fh-NPs simple and doped with Cu and Co, and the effect of these NPs on the thermal denaturation of LDH were monitored. The quenching mechanism is static, the binding occurring with moderate affinity, being mainly driven by hydrogen bonding and van der Waals forces. FRET occurs at a minimal distance of 2.55 nm. Thermal denaturation of LDH in the presence of simple and doped Fh-NPs shows that the thermodynamic parameters of protein unfolding are significantly changed with temperature. The denaturation temperature of LDH shifts to higher values in the presence of all Fh-NPs, than in the case of simple LDH. The docking approach estimates the energy corresponding to the best fit of the ferrihydrite in the LDH binding site near Trp. These results have direct implications on the uses of the complex of LDH with Fh-NPs in various biochemical, biological, or clinical applications. © 2020 Elsevier B.V.

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Издание

Журнал: International Journal of Biological Macromolecules

Выпуск журнала: Vol. 164

Номера страниц: 3559-3567

ISSN журнала: 01418130

Авторы

  • Chilom C.G. (Faculty of Physics, University of Bucharest, Romania)
  • Sandu N. (Faculty of Physics, University of Bucharest, Romania)
  • Bălăşoiu M. (Joint Institute for Nuclear Research, Dubna, Russian Federation, Moscow Institute of Physics and Technology, Dolgoprudniy, Russian Federation, “Horia Hulubei” National Institute of Physics and Nuclear Engineering, Măgurele, Romania)
  • Yaroslavtsev R.N. (Siberian Federal University, Krasnoyarsk, Russian Federation, KirenskyInstitute of Physics, SB RAS, Krasnoyarsk, 660036, Russian Federation)
  • Stolyar S.V. (Siberian Federal University, Krasnoyarsk, Russian Federation, KirenskyInstitute of Physics, SB RAS, Krasnoyarsk, 660036, Russian Federation)
  • Rogachev A.V. (Joint Institute for Nuclear Research, Dubna, Russian Federation, Moscow Institute of Physics and Technology, Dolgoprudniy, Russian Federation)

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