| Autor: |
Lukáčová Bujňáková Z; Institute of Geotechnics, Slovak Academy of Sciences, Watsonova 45, 04001 Košice, Slovakia., Dutková E; Institute of Geotechnics, Slovak Academy of Sciences, Watsonova 45, 04001 Košice, Slovakia., Jakubíková J; Cancer Research Institute of Biomedical Research Center, Slovak Academy of Sciences, Dúbravská Cesta 9, 84505 Bratislava, Slovakia., Cholujová D; Cancer Research Institute of Biomedical Research Center, Slovak Academy of Sciences, Dúbravská Cesta 9, 84505 Bratislava, Slovakia., Varhač R; Faculty of Science, Pavol Jozef Šafárik University in Košice, Šrobárova 2, 04154 Košice, Slovakia., Borysenko L; Chuiko Institute of Surface Chemistry, National Academy of Science of Ukraine, Generala Naumova 17, 03164 Kyiv, Ukraine., Melnyk I; Institute of Geotechnics, Slovak Academy of Sciences, Watsonova 45, 04001 Košice, Slovakia. |
| Abstrakt: |
In this paper, ZnS nanoparticles were bioconjugated with bovine serum albumin and prepared in a form of nanosuspension using a wet circulation grinding. The stable nanosuspension with monomodal particle size distribution (d 50 = 137 nm) and negative zeta potential (-18.3 mV) was obtained. The sorption kinetics and isotherm were determined. Interactions between ZnS and albumin were studied using the fluorescence techniques. The quenching mechanism, describing both static and dynamic interactions, was investigated. Various parameters were calculated, including the quenching rate constant, binding constant, stoichiometry of the binding process, and accessibility of fluorophore to the quencher. It has been found that tryptophan, in comparison to tyrosine, can be closer to the binding site established by analyzing the synchronous fluorescence spectra. The cellular mechanism in multiple myeloma cells treated with nanosuspension was evaluated by fluorescence assays for quantification of apoptosis, assessment of mitochondrial membrane potential and evaluation of cell cycle changes. The preliminary results confirm that the nontoxic nature of ZnS nanoparticles is potentially applicable in drug delivery systems. Additionally, slight changes in the secondary structure of albumin, accompanied by a decrease in α-helix content, were investigated using the FTIR method after analyzing the deconvoluted Amide I band spectra of ZnS nanoparticles conjugated with albumin. Thermogravimetric analysis and long-term stability studies were also performed to obtain a complete picture about the studied system. |
