Insulin and Human Serum Albumin Interactions with Core-Shell Fe3O4@SiO2 Nanoparticles Functionalized with Carboranes
Ludzik K. Marcinkowska M. Klajnert-Maculewicz B. Huang L. Jazdzewska M. Korolkov I.V. Kozlovskiy A.L. Zdorovets M.V. Jasiak N.
10 July 2025American Chemical Society
Journal of Physical Chemistry B
2025#129Issue 276757 - 6764 pp.
In a biological medium, nanoparticles (NPs) can spontaneously interact with proteins, adsorb onto their surface, and cause conformational and orientation changes of the proteins. As a result, the protein function is influenced in a complex manner. Therefore, a detailed understanding of the nature and specificity of protein-nanoparticle interactions is crucial for the application of functional NPs in medicine. In the presented work, we studied the interactions of GMA-treated SiO2 NPs with the Fe3O4 core and attached carborane compounds (Fe3O4/TEOS/TMSPM/GMA/Carborane), designed for boron neutron capture therapy, with human serum albumin (HSA) and insulin. We combined different techniques: spectrofluorometry, circular dichroism spectroscopy, and isothermal titration calorimetry to address this issue. The results show that the adsorption of protein onto the NP surface is enthalpy-entropy-driven, with ensuing structural changes of the protein. As for albumin, the percentage of the α-helix structure in the protein is significantly reduced from 87.59 (free protein) to 40.9% for an NP concentration of 1.8 mg/mL, while the content of the β-sheet and random coil increases from 0.48 to 8.78% and from 11.93 to 50.32%, respectively. The interaction between NPs and small protein-insulin is weaker than that for HSA, confirming less negative ΔH and a 15% decrease in the α-structure content for the highest concentration of NPs. For both proteins, the exposure on Fe3O4/TEOS/TMSPM/GMA/Carborane affects the polarity of the microenvironment around Trp, which is consequently exposed to a more hydrophobic environment. Calculated values of the radius of gyration and the minimum distance between the proteins and the NPs indicate a stronger interaction and closer binding proximity to the NPs, corroborating experimental observations of the higher binding affinity of HSA to NPs.
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Department of Physical Chemistry, University of Lodz, Lodz, 90-236, Poland
Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, 90-237, Poland
School of Sustainable Chemical, Biological and Materials Engineering, University of Oklahoma, Norman, 73019, OK, United States
Department of Experimental Physics of Condensed Phase, Faculty of Physics and Astronomy, Adam Mickiewicz University, Poznan, 61-614, Poland
The Institute of Nuclear Physics, Almaty, 050032, Kazakhstan
Eurasian National University, Astana, 010008, Kazakhstan
Department of Physical Chemistry
Department of General Biophysics
School of Sustainable Chemical
Department of Experimental Physics of Condensed Phase
The Institute of Nuclear Physics
Eurasian National University
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