Publications by authors named "Saba Zendehcheshm"

4 Publications

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Selenium nanoparticles: Synthesis, cytotoxicity, antioxidant activity and interaction studies with ct-DNA and HSA, HHb and Cyt c serum proteins.

Biotechnol Rep (Amst) 2021 Jun 15;30:e00615. Epub 2021 Apr 15.

Center of Medical Biology Research, Health Technology Institute, Kermanshah University of Medical Sciences, Kermanshah, Iran.

The aim of this study was the synthesis of selenium nanoparticles (SeNPs) employing vitamin C as a biocompatible and low toxic reducing agent. The synthesized selenium nanoparticles were characterized by using UV-vis, FT-IR, SEM-EDX, TEM, DLS, and zeta potential measurements. The results of the DPPH free radical scavenging assay demonstrate that this synthesized nano-selenium has strong potentials to scavenge the free radicals and cytotoxicity against MCF-7 and Raji Burkitt's lymphoma cancer cell lines. The interaction of calf thymus DNA (ct-DNA) with SeNPs indicated that the anticancer activity might be associated with the DNA-binding properties of nano-selenium. Finally, it was found that the synthesized nano-selenium can bind to the most important blood proteins such as human serum albumin (HSA), human hemoglobin (HHb), and Cytochrome c (Cyt c). The results showed that the secondary structure of these proteins remains unchanged, suggesting that the synthesized nano-selenium could be employed as a carrier in the drug delivery system without any cytotoxicity effect.
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http://dx.doi.org/10.1016/j.btre.2021.e00615DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8080047PMC
June 2021

Interaction of human hemoglobin (HHb) and cytochrome c (Cyt c) with biogenic chloroxine-conjugated silver nanoflowers: spectroscopic and molecular docking approaches.

J Biomol Struct Dyn 2021 Apr 30:1-12. Epub 2021 Apr 30.

Inorganic Chemistry Department, Faculty of Chemistry, Razi University, Kermanshah, Iran.

In this research, the biological activity of the antibacterial drug Chloroxine-conjugated biogenic AgNPs (COX-AgNPs) was investigated in simulated physiological conditions (pH = 7.40). Different spectroscopic methods such as UV-visible, fluorescence, and circular dichroism spectroscopic and docking simulation were employed to evaluate the structural changes in the most important blood proteins (human hemoglobin (HHb) and Cytochrome c (Cyt c)) in the presence of COX-AgNPs. The results showed that the COX-AgNPs can bind to HHb and Cyt c and the secondary structure of these proteins remains unchanged, which is crucial in providing insights into the side effects of newly synthesized drugs on their carriers.Communicated by Ramaswamy H. Sarma.
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http://dx.doi.org/10.1080/07391102.2021.1919555DOI Listing
April 2021

Evaluation of ct-DNA and HSA binding propensity of antibacterial drug chloroxine: Multi-spectroscopic analysis, atomic force microscopy and docking simulation.

Spectrochim Acta A Mol Biomol Spectrosc 2020 Apr 10;230:118042. Epub 2020 Jan 10.

Department of Inorganic Chemistry, Faculty of Chemistry, Razi University, Kermanshah, Iran.

In the present study, the binding interactions of chloroxine, an antibacterial drug and antibiotic agent with calf thymus-deoxyribonucleic acid (ct-DNA) and human serum albumin (HSA) have been deliberated under simulative physiological conditions (pH = 7.40) employing multiple biophysical, atomic force microscopy and molecular modeling approaches. The ct-DNA binding properties of chloroxine exhibit that it binds to ct-DNA through a groove binding mode, and the binding constant values were computed employing the absorption and emission spectral data. The fluorescence study shows the presence of the static quenching mechanism in the ct-DNA- chloroxine interaction. These results are further supported by UV-vis spectra. Large complexes contain the ct-DNA chains with an average size of 225.45 nm were observed by employing AFM for chloroxine -ct-DNA. The results revealed that the fluorescence quenching of albumin by chloroxine was a static quenching process as a result of albumin-chloroxine (1:1) complex. The distance between chloroxine and albumin was obtained based on the Förster's theory of non-radiative energy transfer. The results of AFM, synchronous and three-dimensional fluorescence spectra all revealed that chloroxine induced the conformational changes of albumin. Molecular docking technology represents the binding of chloroxine to the major groove of ct-DNA and site I (subdomain II A) of albumin.
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http://dx.doi.org/10.1016/j.saa.2020.118042DOI Listing
April 2020

Studies on the Interaction of [SnMeCl(bubpy)] Complex with ct-DNA Using Multispectroscopic, Atomic Force Microscopy (AFM) and Molecular Docking.

Nucleosides Nucleotides Nucleic Acids 2019 11;38(2):157-182. Epub 2019 Mar 11.

a Department of Inorganic Chemistry, Faculty of Chemistry , Razi University , Kermanshah , Iran.

The interaction of SnMeCl(bubpy)complex with calf thymus DNA (ct-DNA) has been explored following, using spectroscopic methods, viscosity measurements, Atomic force microscopy, Thermal denaturation and Molecular docking. It was found that Sn(IV) complex could bind with DNA via intercalation mode as evidenced by hyperchromism and bathochromic in UV-Vis spectrum; these spectral characteristics suggest that the Sn(IV) complex interacts with DNA most likely through a mode that involves a stacking interaction between the aromatic chromophore and the base pairs of DNA. In addition, the fluorescence emission spectra of intercalated methylene blue (MB) with increasing concentrations of SnMeCl(bubpy) represented a significant increase of MB intensity as to release MB from MB-DNA system. Positive values of ΔH and ΔS imply that the complex is bound to ct-DNA mainly via the hydrophobic attraction. Large complexes contain the DNA chains with an average size of 859 nm were observed by using AFM for Sn(IV) Complex-DNA. The Fourier transform infrared study showed a major interaction of Sn(IV) complex with G-C and A-T base pairs and a minor perturbation of the backbone PO group. Addition of the Sn(IV)complex results in a noticeable rise in the Tm of DNA. In addition, the results of viscosity measurements suggest that SnMeCl(bubpy) complex may bind with the classical intercalative mode. From spectroscopic and hydrodynamic studies, it has been found that Sn(IV)complex interacts with DNA by intercalation mode. Optimized docked model of DNA-complex mixture confirmed the experimental results.
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http://dx.doi.org/10.1080/15257770.2018.1506885DOI Listing
May 2019