دورية أكاديمية
Ferrihydrite nanoparticles insights: Structural characterization, lactate dehydrogenase binding and virtual screening assay.
| العنوان: | Ferrihydrite nanoparticles insights: Structural characterization, lactate dehydrogenase binding and virtual screening assay. |
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| المؤلفون: | Chilom CG; Faculty of Physics, University of Bucharest, Romania. Electronic address: claudia.chilom@fizica.unibuc.ro., Sandu N; Faculty of Physics, University of Bucharest, Romania., Bălăşoiu M; Joint Institute for Nuclear Research, Dubna, Russia; Moscow Institute of Physics and Technology, Dolgoprudniy, Russia; 'Horia Hulubei' National Institute of Physics and Nuclear Engineering, Măgurele, Romania., Yaroslavtsev RN; Siberian Federal University, Krasnoyarsk, Russia; KirenskyInstitute of Physics, SB RAS, Krasnoyarsk 660036, Russia., Stolyar SV; Siberian Federal University, Krasnoyarsk, Russia; KirenskyInstitute of Physics, SB RAS, Krasnoyarsk 660036, Russia., Rogachev AV; Joint Institute for Nuclear Research, Dubna, Russia; Moscow Institute of Physics and Technology, Dolgoprudniy, Russia. |
| المصدر: | International journal of biological macromolecules [Int J Biol Macromol] 2020 Dec 01; Vol. 164, pp. 3559-3567. Date of Electronic Publication: 2020 Sep 02. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: Guildford, Eng., IPC Science and Technology Press. |
| مواضيع طبية MeSH: | Ferric Compounds/*chemistry , L-Lactate Dehydrogenase/*chemistry , Nanoparticles/*chemistry, Algorithms ; Chemical Phenomena ; Drug Discovery ; Models, Theoretical ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Molecular Structure ; Protein Binding ; Spectrum Analysis ; Structure-Activity Relationship ; Thermodynamics |
| مستخلص: | 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. (Copyright © 2020 Elsevier B.V. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Binding mechanism; Energy transfer; Ferrihydrite nanoparticles; Lactate dehydrogenase; Thermodynamic fingerprint; Virtual screening |
| المشرفين على المادة: | 0 (Ferric Compounds) 87PZU03K0K (ferric oxyhydroxide) EC 1.1.1.27 (L-Lactate Dehydrogenase) |
| تواريخ الأحداث: | Date Created: 20200905 Date Completed: 20210412 Latest Revision: 20210412 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/j.ijbiomac.2020.08.242 |
| PMID: | 32890566 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1879-0003 |
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| DOI: | 10.1016/j.ijbiomac.2020.08.242 |