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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-24 11:38 |
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Conference: Bucharest University Faculty of Physics 2021 Meeting
Section: Biophysics; Medical Physics
Title:
Spectroscopic and molecular docking study of interactions between chemically synthesized ferrihydrite nanoparticles and human serum transferrin
Authors:
Nicoleta SANDU (1), Claudia CHILOM (1), Sorina IFTIMIE (1), Maria BĂLĂȘOIU (2,3,4), Andrey ROGACHEV (2,4), Oleg ORELOVICH (2), Sergey STOLYAR (5)
*
Affiliation:
1) Department of Electricity, Solid Physics and Biophysics, Faculty of Physics, University of Bucharest, Măgurele, Romania;
2) Joint Institute for Nuclear Research, Dubna, Russia
3) Horia Hulubei National Institute for R&D in Physics and Nuclear Engineering, Măgurele, Romania
4) Moscow Institute of Physics and Technology, Dolgoprudniy, Russia
5) Krasnoyarsk Scientific Center, Federal Research Center KSC SB RAS Krasnoyarsk, Russia
E-mail
s.nicoleta59@yahoo.ro
Keywords:
ferrihydrite nanoparticles, human serum transferrin, binding mechanism, molecular docking
Abstract:
Human serum transferrin (HST) is a glycoprotein that binds and transports iron and other ligands such as flavonoids and vitamins in human plasma. Considering this aspect in this study the interaction between HST and simple ferrihydrite nanoparticles (Fh-NPs) but also doped with cobalt (Co) and copper (Cu) was analyzed by spectroscopic and molecular docking approaches. Fluorescence spectroscopy and molecular docking studies revealed that Fh-NPs bind with a low affinity to HST characterized by a static quenching mechanism of the fluorescence of the HST by the simple Fh-NPs and a combined mechanism for the NPs doped with Co and Cu. Fluorescence resonance energy transfer (FRET) allowed the estimation of the distances between the donor (HST) and the acceptors (Fh-NPs). The distance estimated between the donor (HST) and the acceptor (Fh-NPs) in the range of 3.10 - 3.23 nm is less than 7 nm which indicates that the energy transfer occurs with high probability between HST and nanoparticles. To establish the stability of the apo-HST and HST-NPs at different temperatures the denaturation temperature (Tm) was determined. The results obtained almost the same transition of temperature for all HST-NPs complexes, but the presence of NPs seems to increase the protein stability.
The biophysical effect of Fh-NPs on serum proteins can be an important step in their use in biological applications as hyperthermia, drug targeting, and diagnostic applications.
Acknowledgement:
The work was accomplished with the financial support of the RO-JINR Projects No. 365/11.05.2021, items 8, 87 and 98 and respectively, No. 366/11.05.2021, items 7, 86 and 97.
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