| Autor: |
Shekhar H; Biophysical and Protein Chemistry Lab, Department of Chemistry, National Institute of Technology, Rourkela, India., Behera P; Neural Developmental Biology Lab, Department of Life Science, National Institute of Technology, Rourkela, India., Naik A; Biophysical and Protein Chemistry Lab, Department of Chemistry, National Institute of Technology, Rourkela, India., Mishra M; Neural Developmental Biology Lab, Department of Life Science, National Institute of Technology, Rourkela, India., Sahoo H; Biophysical and Protein Chemistry Lab, Department of Chemistry, National Institute of Technology, Rourkela, India.; Center for Nanomaterials, National Institute of Technology, Rourkela, India. |
| Jazyk: |
angličtina |
| Zdroj: |
Nanotoxicology [Nanotoxicology] 2024 Aug; Vol. 18 (5), pp. 479-498. Date of Electronic Publication: 2024 Aug 23. |
| DOI: |
10.1080/17435390.2024.2392579 |
| Abstrakt: |
Iron oxide nanoparticles (IONPs) have been extensively explored in biomedicine, bio-sensing, hyperthermia, and drug/gene delivery, attributed to their versatile and tunable properties. However, owing to its numerous applications, the functionalization of IONPs with appropriate materials is in demand. To achieve optimal functionalization of IONPs, polydopamine (PDA) was utilized due to its ability to provide a superior functionalized surface, near-infrared light absorption, and adhesive nature to customize desired functionalized IONPs. This notion of involving PDA led to the successful synthesis of magnetite-PDA nanoparticles, where PDA is surface-coated on magnetite (Fe 3 O 4 @PDA). The Fe 3 O 4 @PDA nanoparticles were characterized using techniques like TEM, FESEM, PXRD, XPS, VSM, and FTIR, suggesting PDA's successful attachment with magnetite crystal structure retention. Human serum albumin (HSA), the predominant protein in blood plasma, interacts with the delivered nanoparticles. Therefore, we have employed various spectroscopic techniques, along with cytotoxicity, to inspect the effect of Fe 3 O 4 @PDA NPs on the stability and structure of HSA. The structural alterations were examined using circular dichroism (CD) and synchronous fluorescence spectroscopy (SFS). It has been observed that there are no structural perturbations in the secondary structure of the HSA protein after interaction with Fe 3 O 4 @PDA. Studies using steady-state fluorescence revealed that the inherent fluorescence intensities of HSA were suppressed after interaction with Fe 3 O 4 @PDA. In addition, temperature-dependent fluorescence measurements suggested that the type of quenching consists of both static and dynamic quenching simultaneously. A cytotoxicity study in Drosophila melanogaster larvae revealed no cytotoxic effects but did show a minor genotoxic effect only at higher concentrations. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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