Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies
Human serum transferrin (HST) is a glycoprotein involved in iron transport that may be a candidate for functionalized nanoparticles to bind and target cancer cells. In this study, the effects of the simple and doped with cobalt (Co) and copper (Cu) ferrihydrite nanoparticles (Fh-NPs, Cu-Fh-NPs, and...
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MDPI AG
2021-06-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/13/7034 |
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| author | Claudia G. Chilom Nicoleta Sandu Sorina Iftimie Maria Bălăşoiu Andrey Rogachev Oleg Orelovich Sergey Stolyar |
| author_facet | Claudia G. Chilom Nicoleta Sandu Sorina Iftimie Maria Bălăşoiu Andrey Rogachev Oleg Orelovich Sergey Stolyar |
| author_sort | Claudia G. Chilom |
| collection | DOAJ |
| description | Human serum transferrin (HST) is a glycoprotein involved in iron transport that may be a candidate for functionalized nanoparticles to bind and target cancer cells. In this study, the effects of the simple and doped with cobalt (Co) and copper (Cu) ferrihydrite nanoparticles (Fh-NPs, Cu-Fh-NPs, and Co-Fh-NPs) were studied by spectroscopic and molecular approaches. Fluorescence spectroscopy revealed a static quenching mechanism for all three types of Fh-NPs. All Fh-NPs interacted with HST with low affinity, and the binding was driven by hydrogen bonding and van der Waals forces for simple Fh-NPs and by hydrophobic interactions for Cu-Fh-NPs and Co-Fh-NPs binding, respectively. Of all samples, simple Fh-NPs bound the most to the HST binding site. Fluorescence resonance energy transfer (FRET) allowed the efficient determination of the energy transfer between HST and NPs and the distance at which the transfer takes place and confirmed the mechanism of quenching. The denaturation of the HST is an endothermic process, both in the case of <i>apo</i> HST and HST in the presence of the three types of Fh-NPs. Molecular docking studies revealed that Fh binds with a low affinity to HST (<i>K<sub>a</sub></i> = 9.17 × 10<sup>3</sup> M<sup>−1</sup>) in accord with the fluorescence results, where the interaction between simple Fh-NPs and HST was described by a binding constant of 9.54 × 10<sup>3</sup> M<sup>−1</sup>. |
| first_indexed | 2024-03-09T04:44:20Z |
| format | Article |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T04:44:20Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-cf847b2508994bd685ad9c6228c7f11f2023-12-03T13:17:26ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-06-012213703410.3390/ijms22137034Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic StudiesClaudia G. Chilom0Nicoleta Sandu1Sorina Iftimie2Maria Bălăşoiu3Andrey Rogachev4Oleg Orelovich5Sergey Stolyar6Department of Electricity, Solid Physics and Biophysics, Faculty of Physics, University of Bucharest, Str Atomistilor 405, CP MG 11, RO-077125 Măgurele, RomaniaDepartment of Electricity, Solid Physics and Biophysics, Faculty of Physics, University of Bucharest, Str Atomistilor 405, CP MG 11, RO-077125 Măgurele, RomaniaDepartment of Electricity, Solid Physics and Biophysics, Faculty of Physics, University of Bucharest, Str Atomistilor 405, CP MG 11, RO-077125 Măgurele, RomaniaJoint Institute for Nuclear Research, Joliot-Curie No. 6, 141980 Dubna, RussiaJoint Institute for Nuclear Research, Joliot-Curie No. 6, 141980 Dubna, RussiaJoint Institute for Nuclear Research, Joliot-Curie No. 6, 141980 Dubna, RussiaKrasnoyarsk Science Center of the Siberian, Branch of the Russian Academy of Sciences, Akademgorodok St. No. 50, 660036 Krasnoyarsk, RussiaHuman serum transferrin (HST) is a glycoprotein involved in iron transport that may be a candidate for functionalized nanoparticles to bind and target cancer cells. In this study, the effects of the simple and doped with cobalt (Co) and copper (Cu) ferrihydrite nanoparticles (Fh-NPs, Cu-Fh-NPs, and Co-Fh-NPs) were studied by spectroscopic and molecular approaches. Fluorescence spectroscopy revealed a static quenching mechanism for all three types of Fh-NPs. All Fh-NPs interacted with HST with low affinity, and the binding was driven by hydrogen bonding and van der Waals forces for simple Fh-NPs and by hydrophobic interactions for Cu-Fh-NPs and Co-Fh-NPs binding, respectively. Of all samples, simple Fh-NPs bound the most to the HST binding site. Fluorescence resonance energy transfer (FRET) allowed the efficient determination of the energy transfer between HST and NPs and the distance at which the transfer takes place and confirmed the mechanism of quenching. The denaturation of the HST is an endothermic process, both in the case of <i>apo</i> HST and HST in the presence of the three types of Fh-NPs. Molecular docking studies revealed that Fh binds with a low affinity to HST (<i>K<sub>a</sub></i> = 9.17 × 10<sup>3</sup> M<sup>−1</sup>) in accord with the fluorescence results, where the interaction between simple Fh-NPs and HST was described by a binding constant of 9.54 × 10<sup>3</sup> M<sup>−1</sup>.https://www.mdpi.com/1422-0067/22/13/7034ferrihydrite nanoparticleshuman serum transferrinbinding mechanismdriving forcesmolecular docking |
| spellingShingle | Claudia G. Chilom Nicoleta Sandu Sorina Iftimie Maria Bălăşoiu Andrey Rogachev Oleg Orelovich Sergey Stolyar Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies International Journal of Molecular Sciences ferrihydrite nanoparticles human serum transferrin binding mechanism driving forces molecular docking |
| title | Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies |
| title_full | Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies |
| title_fullStr | Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies |
| title_full_unstemmed | Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies |
| title_short | Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies |
| title_sort | interactions of chemically synthesized ferrihydrite nanoparticles with human serum transferrin insights from fluorescence spectroscopic studies |
| topic | ferrihydrite nanoparticles human serum transferrin binding mechanism driving forces molecular docking |
| url | https://www.mdpi.com/1422-0067/22/13/7034 |
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