Synthesis of Silica Based Nanoparticles Against the Proliferation of Human Prostate Cancer.

BACKGROUND: Prostate cancer (PCa) has the second-highest morbidity and mortality rates in men. Possessing facile surface chemistry and unique optical properties make silica nanoparticles(SiO2-NPs) promising cancer therapy materials. OBJECTIVE: This study aimed to investigate the effects of SiO2-NPs and their derivatives, including SiNP-NH2, SiNP-Cl, and SiNP-SH against PCa and clarify their molecular mechanism on cell death, gene, and protein expressions. METHODS: Following the synthesis and derivation of SiO2-NPs, their characterization was carried out using TEM, DLS, BET, and FT-IR. Cytotoxic properties of the compounds were investigated against different human cancerous cells; including HUH-7, A549, DLD-1, HeLa, NCI-H295R, and PC-3, as well as human healthy epithelium cell line PNT1A. RESULTS: SiNP-NH2, SiNP-Cl, and SiNP-SH dose-dependently inhibited the proliferation of PC-3 cells with an IC50 value as 55.46 µg/mL, 55.09 µg/mL and 72.89 µg/mL, respectively. SiNP-SH significantly(p<0.0001) inhibited metastasis and invasion of PC-3 cells(20.4% and 46.7%, respectively), and significantly(p<0.0001) increased early apoptosis(32.3%) when compared with non-treated cells. Protein and mRNA expressions of BcL-2, Bax, caspase-3, caspase-9, caspase-12, p53, Smad-4, Kras, and Nf-ĸB were also altered following the treatment of SiO2-NPs and its derivatives. CONCLUSION: Our results demonstrated that -SH functioned SiO2-NPs can prevent the proliferation of human PCa by increasing apoptosis by up-regulating gene and protein expression of p53(TP53) as well as caspase-3, caspase-9, and caspase-12 in the apoptotic pathway. Besides, the increased level of Smad-4 has also implicated the decreased cell proliferation. Hence, low sized SiNP-SH nanoparticles might be a suitable candidate for the treatment of human PCa.

Urease immobilized electrospun PVA/chitosan nanofibers with improved stability and reusability characteristics: an application for removal of urea from artificial blood serum.

Electrospun polyvinyl alcohol (PVA)/Chitosan nanofibers were successfully prepared and were used as carriers for the first time in urease immobilization. Also, urease immobilized electrospun PVA/Chitosan nanofibers were applied for the removal of urea from artificial blood serum by recycled reactor. The nanofibers were optimized and synthesized by electrospinning technique according to the operational parameters. The morphology and structure of the nanofibers were characterized by scanning electron microscopy (SEM), attenuated total reflection-Fourier transform infrared spectroscopy (ATR-FTIR) and thermogravimetric analysis (TGA). Urease was immobilized on the nanofibers by adsorption and crosslinking methods. According to immobilization results, nanofiber enhanced urease stability properties like thermal stability, pH stability, and reusability. Urease immobilized electrospun PVA/Chitosan nanofiber protected its activity by 85% after 10 uses and 45% after 20 uses. Urea removal rates of artificial blood serum were as follows: 100% at 1st cycle, 95% at 2nd, 3rd and 4th cycles; 85% at the 5th cycle; 76% at the 6th cycle, and 65% at the last three cycles.

Synthesis and characterization of electrospun PVA/Zn2+ metal composite nanofibers for lipase immobilization with effective thermal, pH stabilities and reusability.

Polyvinyl alcohol (PVA)/Zn2+ electrospun nanofibers that were a kind of polymer/ionic metal composite was successfully embedded in the hybrid fibers for the first time in the literature, due to chemical interactions between PVA and Zn2+. Also, the nanofibers were used as carriers for the first time in enzyme immobilization. The nanofibers were optimized and synthesized by electrospinning technique according to the operational parameters like as PVA concentration (%), Zn2+ concentration (%), voltage (kV), needle tip-collector distance (cm) and injection speed (ml/h). The morphology and structure of the nanofibers were characterized by SEM, XRD, ATR-FTIR and TGA. Lipase was immobilized on the nanofibers by adsorption and crosslinking methods. According to immobilization results, nanofiber enhanced enzyme stability properties like as thermal stability, pH stability and reusability. Lipase immobilized nanofiber protected 90% of its activity after 14 reuses.

Performance of SiO2/Ag Core/Shell particles in sonocatalalytic degradation of Rhodamine B.

In this study, SiO2/Ag Core/Shell nanoparticles was prepared and sonocatalytic activity of prepared catalyst was investigated by using Rhodamine B as model contaminant, at 35 kHz using ultrasonic power of 160 W within 90 min. The change in efficiency in the sonocatalytic degradation of Rhodamine B catalyzed by SiO2/Ag Core/Shell nanoparticles with respect to the initial concentration of dye, catalyst amount and temperature were firstly investigated. Optimal conditions were found as follows: catalyst amount = 15 mg/L, Temperature = 25 °C and initial concentration of dye = 10 ppm. Influence factors such as pH of solution, O2 saturation of solution and the concentration of H2O2 added to the solution, on degradation efficiency in presence of catalyst, were investigated. SiO2/Ag Core/Shell nanoparticles showed higher sonocatalytic activity at pH = 7 with respect to acidic and alkaline conditions. Degradation efficiency was reached up to 67% in experiments which air pumped (0.6 L/min) through the solution with in 90 min. It was observed that the dye removal increased via increase while H2O2 concentration lower than 10 mM. Higher concentration of H2O2 than the optimal concentration had adverse effect on degradation efficiency. Our results showed that the SiO2/Ag Core/Shell nanoparticles were active catalyst for sonocatalytic degradation of dyes. Reusability of the catalyst was investigated.

A comparative study for lipase immobilization onto alginate based composite electrospun nanofibers with effective and enhanced stability.

In this study, lipase was successfully immobilized on polyvinyl alcohol/alginate and polyethylene oxide/alginate nanofibers that were prepared by electrospinning. Results showed that nanofibers (especially polyvinyl alcohol/alginate) enhanced the stability properties of lipase. When the free lipase lost its all activity after 40-60min at high temperatures, both lipase immobilized nanofibers kept almost 65-70% activity at the same time. The lipase immobilized poly vinyl alcohol/alginate and polyethylene oxide/alginate nanofibers protected approximately all of their activities until pH 9. Lipase immobilized polyvinyl alcohol/alginate and polyethylene oxide/alginate nanofibers maintained 60% of their activities after 14 and 7 reuses, respectively. The morphology of nanofibers was characterized by Scanning Electron Microscope, Fourier Transform Infrared Spectroscopy and Thermal Gravimetric Analyzer. As a result, this nanofiber production method, electrospinning, is simple, versatile and economical for preparing appropriate carrier to immobilize the enzymes.

Synthesis and characterization of chitosan/TiO2 composite beads for improving stability of porcine pancreatic lipase.

The purpose of the present work is improving stability properties of porcine pancreatic lipase (triacylglycerol lipase, E.C.3.1.1.3) by immobilization on chitosan/TiO2 composite beads. The immobilization parameters were initial enzyme concentration (0.5-2 mg/ml), adsorption time (5-25 min), and glutaraldehyde concentration (1-4 % v/v). The optimum temperature (20-60 °C), optimum pH (3.0-10.0), kinetic parameters, thermal stability (4-70 °C), pH stability (4.0-9.0), and reusability (9 times) were investigated for characterization of immobilized lipase system. The optimum temperatures of free and immobilized lipase were 30 °C. The temperature profile of the immobilized lipase was spread over a large area. The optimum pH values for the free lipase and immobilized lipase were found to be 6.5 and 7.5, respectively. The thermal stability of immobilized lipase was evaluated, and it maintained 45 % activity at 70 °C. But, at this temperature, soluble lipase protected only 15 % activity. Also, the structural characterization of chitosan/TiO2 composite beads was analyzed with scanning electron microscope (SEM), X-ray diffraction (XRD), thermal gravimetric analysis (TGA), and attenuated total reflection Fourier transform infrared spectroscopy analysis (ATR-FTIR). The significance of this study is improving of stability properties of lipase for the industrial usage especially production of biodiesel and dairy products.

TiO2 beads and TiO2-chitosan beads for urease immobilization.

The aim of the present study is to synthesize TiO2 beads for urease immobilization. Two different strategies were used to immobilize the urease on TiO2 beads. In the first method (A), urease enzyme was immobilized onto TiO2 beads by adsorption and then crosslinking. In the second method (B), TiO2 beads were coated with chitosan-urease mixture. To determine optimum conditions of immobilization, different parameters were investigated. The parameters of optimization were initial enzyme concentration (0.5; 1; 1.5; 2mg/ml), alginate concentration (1; 2; 3%), glutaraldehyde concentration (1; 2; 3% v/v) and chitosan concentration (2; 3; 4 mg/ml). The optimum enzyme concentrations were determined as 1.5mg/ml for A and 1.0mg/ml for B. The other optimum conditions were found 2.0% (w/v) for alginate concentration (both A and B); 3.0mg/ml for chitosan concentration (B) and 2.0% (v/v) for glutaraldehyde concentration (A). The optimum temperature (20-60°C), optimum pH (3.0-10.0), kinetic parameters, thermal stability (4-70°C), pH stability (4.0-9.0), operational stability (0-230 min) and reusability (20 times) were investigated for characterization. The optimum temperatures were 30°C (A), 40°C (B) and 35°C (soluble). The temperature profiles of the immobilized ureases were spread over a large area. The optimum pH values for the soluble urease and immobilized urease prepared by using methods (A) and (B) were found to be 7.5, 7.0, 7.0, respectively. The thermal stabilities of immobilized enzyme sets were studied and they maintained 50% activity at 65°C. However, at this temperature free urease protected only 15% activity.