Publications by authors named "Maryam Maghsudi"

Human Serum Albumin, a plasma protein existing in abundance, was selected as a template and reducing agent for the formation of CdNCs due to two factors: its stability and low cost. In the presence of human serum albumin (HSA), a selective and sensitive, low-cost, environmental friendly, and label-free off-on fluorescent sensor was synthesized and characterized for a bioaccumulating and toxic heavy metal, Hg and biothiols. HSA - CdNCs can specifically recognize Hg through aggregating NCs and causing fluorescence quenching.

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The interaction of the cefobiprole drug with calf thymus DNA (ct-DNA) at physiological pH was investigated by UV-visible spectrophotometry, fluorescence measurement, dynamic viscosity measurements, circular dichroism spectroscopy and molecular modeling. The binding constant obtained of UV-visible was 4 × 10 L mol. Moreover, the results of circular dichroism (CD) and viscosity measurements displayed that the binding of the cefobiprole to ct-DNA can change the conformation of ct-DNA.

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In recent years, concerns have been raised considering the potential risks of nanocluster (NC) for the environment and human health. Since the blood circulation system is probably the first entry route of NC into the human body, adsorption of blood proteins on NC may change cellular responses, including cellular uptake efficiency, bio distribution patterns, and nanotoxicity profiles, besides other biological effects. Therefore, the interaction of NCs with proteins and the cellular implications can be therapeutically of great importance.

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The interaction of anticancer drug cytarabine with calf thymus DNA (CT-DNA) was investigated in vitro under simulated physiological conditions by multispectroscopic techniques and molecular modeling study. The fluorescence spectroscopy and UV absorption spectroscopy indicated drug interacted with CT-DNA in a groove-binding mode, while the binding constant of UV-vis and the number of binding sites were 4.0 ± 0.

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We reported the study of calf thymus DNA (ct-DNA) adsorption by the polymer of methyldopa (2-amino-3-(3,4-dihydroxyphenyl)-2-methyl acid, propanoic) (PMDP), magnetofluorescent PMDP-γ-Fe2O3 nanocrystal. The method is based on the extraordinarily high quenching efficiency of ct-DNA and the specific interaction between ct-DNA and PMDP-γ-Fe2O3 via guanine base and metal coordination, probably. It was found that the designed magnetic nanoparticles can adsorb ct-DNA in nM levels in the presence of NaCl and KCl.

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Understanding and controlling the interaction between the polymer methyldopa (2-amino-3-(3,4-dihydroxyphenyl)-2-methyl-propanoic acid) (PMDP)-γ-Fe2 O3 nanoparticles and biological fluids is important if the potential of nanoparticles (NPs) in biomedicine is to be realized. Physicochemical studies on the interactions between proteins and NPs are influenced by the surface properties of the NPs. To identify the effects of the NP surface, interactions between human serum albumin (HSA) and PMDP-γ-Fe2 O3 NPs were investigated.

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One of the most important aspects of the biological systems is the retention of HSA activity. It is known that serum albumin, in addition to ligand binding capabilities, possesses some enzymatic properties such as esterase activity with p-nitrophenyl acetate substrate. The aim of this study was to synthesize and characterize the mono-dispersed magneto-fluorescent methyldopa coated (MNPs-MDP) which provides a unique opportunity to control and monitor the biological interactions by using magnetic force.

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The interaction of methyldopa [(S)-2-amino-3-(3,4-dihydroxyphenyl)-2-methyl propanoic acid] (MDP), antihypertensive drug, with calf thymus DNA (ct-DNA) was investigated by spectroscopic and viscometric techniques. According to the results arising from the fluorescence spectra, viscosity measurements and molecular modeling studies; we concluded that MDP is a minor groove binder of ct-DNA and preferentially binds to AT rich regions. Ethidium bromide (EB) displacement studies revealed that MDP did not have any effect on EB bound DNA which is indicative of groove binding.

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The interaction of a food colourant, quinoline yellow (Qy), and bovine serum albumin (BSA) was investigated by spectrophotometry, spectrofluorometry, FT-IR and circular dichroism (CD) techniques. The experimental results indicated that the quenching mechanism of BSA by the dye was a static procedure. Various binding parameters were evaluated.

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The interaction of silver(I) complex, [Ag (2,9-dimethyl-1,10-phenanthroline)(2)](NO(3))·H(2)O, and bovine serum albumin (BSA) was investigated by spectrophotometry, spectrofluorimetry and circular dichroism (CD) techniques. The experimental results indicated that the quenching mechanism of BSA by the complex was a static procedure. Various binding parameters were evaluated.

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One approach to accelerate the availability of new cancer drugs is to test drugs approved for other conditions as anticancer agents. In recent years, some researchers have shown that antiviral drugs, such as ritonavir, saquinavir, and nelfinavir, inhibit the growth of over 60 cancer cell lines derived from nine different tumor types. This article studied the anticancer potential of an antiviral drug, lamivudine (LA).

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The interaction of a novel mixed ligand copper (II) complex, [Cu(N-N)(L)(EtOH)](NO(3))(2) . 2H(2)O, in which N-N indicates 2,9-dimethyl-1,10-phenanthroline and L indicates N,N-dimethyltrimethylenediamine with calf thymus DNA was investigated by absorption, circular dichroism, voltammetric, and viscosimetric techniques. The absorption spectra of the complex with calf thymus DNA showed a marked hypochromism in the pi --> pi* and metal to ligand charge transfer (MLCT) transitions, with no obvious red shift attributed to a partial intercalation.

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