Potent carbonic anhydrase I, II, IX and XII inhibition activity of novel primary benzenesulfonamides incorporating bis-ureido moieties.

A novel series of twelve aromatic bis-ureido-substituted benzenesulfonamides was synthesised by conjugation of aromatic aminobenzenesulfonamides with aromatic bis-isocyanates. The obtained bis-ureido-substituted derivatives were tested against four selected human carbonic anhydrase isoforms (hCA I, hCA II, hCA IX and hCA XII). Most of the new compounds showed an effective inhibitory profile against isoforms hCA IX and hCA XII, also having some selectivity with respect to hCA I and hCA II. The inhibition constants of these compounds against isoforms hCA IX and XII were in the range of 6.73-835 and 5.02-429 nM, respectively. Since hCA IX and hCA XII are important drug targets for anti-cancer/anti-metastatic drugs, these effective inhibitors reported here may be considered of interest for cancer related studies in which these enzymes are involved.

Bioactive sulfonyl hydrazones with alkyl derivative: Characterization, ADME properties, molecular docking studies and investigation of inhibition on choline esterase enzymes for the diagnosis of Alzheimer's disease.

In this work, new sulfonylhydrazone compounds with alkyl derivatives (SH1- SH4 series) were synthesized via a green chemistry method, and their inhibition effects on acetylcholinesterase and butyrylcholinesterase (AChE, BChE) were determined in vitro. This work was designed in two stages; in the first stage, using compounds that contain both sulfonamide and hydrazine groups which have important pharmacological properties, a series of sulfonyl hydrazone with alkyl derivatives (SH1- SH4) were synthesized with a method that is less time-consuming and more environmentalist that was by using different substitute groups containing aldehyde and ketone compounds. The structures of the synthesized compounds were characterized by elemental analyses, 1H NMR, 13C NMR, FT-IR methods. In the second stage, the effects of the synthesized sulfonyl hydrazones with alkyl derivatives on acetylcholinesterase and butyrylcholinesterase enzymes were examined. According to the results, all the synthesized compounds inhibited AChE and BChE enzymes. When the IC50 values were compared, SH2-3 (IC50 = 5.27 ± 0.05 µM) and SH3-3 (IC50 = 12.29 ± 1.47 µM) compounds which are containing the butyl group have the best inhibition effect on the AChE enzyme and BChE enzyme, respectively. In addition, the predictive properties of all compounds in terms of drug similarity were scanned using five Lipinski rules and ADME estimations. In silico ADME studies play an important role in improving and predicting drug compounds. In the ADME study; The absorption, distribution, metabolism, elimination, and properties of the molecules given below were theoretically calculated. Also, to evaluate the binding interactions between the sulfonylhydrazone compounds and enzymes, molecular docking studies were performed and the compounds with the best inhibition effect SH2-3 (for AChE enzyme) and SH3-3 (for BChE enzyme) were tested. Both in vitro and silico the results showed that two compounds could act as potent inhibitors of AChE, BChE.

Extraction and quantification of some valuable flavonoids from pinecone of Pinus brutia via Soxhlet and Supercritical CO2 extraction: a comparison study.

In this study, the extraction of oil from pinecone of Pinus brutia was evaluated by supercritical CO2 (Sc-CO2) and Soxhlet extraction methods. The quercetin, rutin and kaempferol (QRK) contents of oil were analyzed one by one via HPLC. The rutin compound investigated in this study has the potential to be a drug against the COVID 19 virus. SEM and BET analysis were performed to observe the structural change and increase in surface area after Sc-CO2 extraction. The operating conditions were investigated in the range of 35-65 °C temperatures, 140-220 bar of pressures, 0.30-1.00 mm of mean particle sizes, 3-7 l/min of CO2 flow rates, 0-8% w/w co-solvent and 30-150 min extraction periods. When the results obtained by the Sc-CO2 method were compared with the results of Soxhlet extraction method, the maximum recovery of total QRK was found 4.18% in co-solvent-free studies and 30.94% in co-solvent-added Sc-CO2 studies. Sc-CO2 extraction results of Q, R, and K were found as 14.75 ± 1.08 µg/g, 14.23 ± 1.27 µg/g, and 15.70 ± 1.13 µg/g pinecone, respectively. Soxhlet extraction results of Q, R, and K were found as 36.43 ± 2.26 µg/g, 57.19 ± 3.81 µg/g, and 50.80 ± 2.79 µg/g pinecone, respectively. The maximum amount of QRK was found as 44.68 ± 2.89 µg/g pinecone by Sc-CO2 method via adding 8% ethanol by mass and as 144.42 ± 5.39 µg/g pinecone by Soxhlet method. According to the reference Soxhlet method efficiency, the Sc-CO2 extraction recovery was found as 30.94%. Supplementary Information: The online version contains supplementary material available at 10.1007/s11696-021-01644-5.

Development of a novel biosensor based on a polypyrrole-dodecylbenzene sulphonate (PPy-DBS) film for the determination of amperometric cholesterol.

Herein a novel amperometric biosensor based on a conducting polymer with anionic dopant modified electrode was successfully developed for detection of cholesterol. Polypyrrole is deposited on a platinum surface and the sodium dodecylbenzene sulphonate (DBS) ion-doped polypyrrole film was electrochemically prepared by scanning the electrode potential between -0.8 and +0.8 V at a scan rate of 20 mV/s. The present electrochemical biosensor was optimized in terms of working potential, number of cycles, concentrations of monomer, and anionic dopant. Cholesterol oxidase (ChOx) was physically entrapped in PPy-DBS to construct an amperometric cholesterol biosensor. Amperometric determination is based on the electrochemical detection of H2O2 generated in the enzymatic reaction of cholesterol. Kinetic parameters, operational and storage stabilities, pH, and temperature dependencies were determined. Km and Imax were calculated as 0.11 µM and 0.967 nM/min, respectively. The operational stability results showed that 90.0% of the response current was retained after 30 activity assays. Morphology of electrodes was characterized by SEM and AFM. Additionally, contact angle measurements were made with 1 µL water of polymer film and enzyme electrode. As a result, the cholesterol biosensor suggested in this study is easy to prepare and is highly cost-effective. This composite (PPy-DBS) can supply a biocompatible and electrochemical microenvironment for immobilization of the enzyme, making this material a good candidate for the fabrication of highly sensitive and selective cholesterol biosensors.

Preparation of Pt/polypyrrole-para toluene sulfonate hydrogen peroxide sensitive electrode for the utilizing as a biosensor.

A film electrode with electropolymerization of pyrrole (Py) and para-toluene sulfonate (pTS) as a anionic dopant is prepared and its sensitivity to hydrogen peroxide is investigated. The polypyrrole is deposited on a 0.5 cm(2) Pt plate an electrochemically prepared pTS ion-doped polypyrrole film by scanning the electrode potential between - 0.8 and + 0.8 V at a scan rate of 20 mV/s. The electrode's sensitivity to hydrogen peroxide is investigated at room temperature using 0.1 M phosphate buffer at pH 7.5. The working potential is found as a 0.3 V. The concentrations of pyrrole and pTS are 50mM M and 25 mM. Polypyrrole was coated on the electrode surface within 10 cycles. Immobilization of glucose oxidase carried out on Pt/polypyrrole-para toluene sulfonate (Pt/PPy-pTS) film by cross-linking with glutaraldehyde. The morphology of electrodes was characterized by SEM and AFM. Moreover, contact angle measurements were made with 1 µL water of polymer film and enzyme electrode. It has shown that enzyme electrode is very sensitive against to glucose.

Preparing a new biosensor for hypoxanthine determination by immobilization of xanthine oxidase and uricase in polypyrrole-polyvinyl sulphonate film.

In this study, a new amperometric biosensor for the determination of hypoxanthine was developed. To this aim, polypyrrole-polyvinyl sulphonate films were prepared on the platinum electrode by the electropolymerization of pyrrole in the presence of polyvinyl sulphonate. Xanthine oxidase and uricase enzymes were immobilized in polypyrrole-polyvinyl sulphonate via the entrapment method. Optimum conditions of enzyme electrode were determined. Hypoxanthine detection is based on the oxidation of hydrogen peroxide at +400 mV produced by the enzymatic reaction on the enzyme electrode surface. The linear working range of biosensor for hypoxanthine was determined. The effects of pH and temperature on the response of the hypoxanthine biosensor were investigated. Optimum pH and temperature were measured as 8 and 30°C, respectively. Operational and storage stability of the biosensor were determined. After 20 assays, the biosensor sustained 74.5% of its initial performance. After 33 days, the biosensor lost 36% of its initial performance. The performance of the biosensor was tested in real samples.

Glucose biosensor based on the immobilization of glucose oxidase on electrochemically synthesized polypyrrole-poly(vinyl sulphonate) composite film by cross-linking with glutaraldehyde.

In this study, a novel amperometric glucose biosensor was developed by immobilizing glucose oxidase (GOX) by cross-linking via glutaraldehyde on electrochemically polymerized polypyrrole-poly(vinyl sulphonate) (PPy-PVS) films on the surface of a platinum (Pt) electrode. Electropolymerization of pyrrole and poly(vinyl sulphonate) on the Pt surface was carried out with an electrochemical cell containing pyrrole and poly(vinyl sulphonate) by cyclic voltammetry between -1.0 and + 2.0 V (vs.Ag/AgCl) at a scan rate of 50 mV/s upon the Pt electrode. The amperometric determination was based on the electrochemical detection of H(2)O(2) generated in enzymatic reaction of glucose. Determination of glucose was carried out by the oxidation of enzymatically produced H(2)O(2) at 0.4 V vs. Ag/AgCl. The effects of pH and temperature were investigated and optimum parameters were found to be 7.5 and 65°C, respectively. The effect of working potential was investigated and optimum potential was determined to be 0.4 V. The operational stability of the enzyme electrode was also studied. The response of the PPy/PVS-GOX glucose biosensor exhibited good reproducibility with a relative standard deviation (RSD) of 2.48%. The glucose biosensor retained 63% of initial activity after 93 days when stored in 0.1 M phosphate buffer solution of pH 7.5 at 4°C. With the low operating potential, the biosensor demonstrated little interference from the possible interferants.

An amperometric biosensor for fish freshness detection from xanthine oxidase immobilized in polypyrrole-polyvinylsulphonate film.

A new amperometric biosensor was developed for determining hypoxanthine in fish meat. Xanthine oxidase with pyrrole and polyvinylsulphonate was immobilized on the surface of a platinum electrode by electropolymerization. The determination of xanthine-hypoxanthine was performed by means of oxidation of uric acid liberated during the enzyme reaction on the surface of the enzyme electrode at + 0.30V (SCE). The effects of pH, substrate concentration, and temperature on the response of the xanthine-hypoxanthine biosensor were investigated. The linear working range of the enzyme electrode was 1.0 × 10(-7) -1.0 × 10(-3) M of the hypoxanthine concentration, and the detection limit was 1.0 × 10(-7)M. The apparent K(m(app)) and I(max) of the immobilized xanthine oxidase were found to be 0.0154 mM and 1.203 µA/mM, respectively. The best pH and temperature value for xanthine oxidase were selected as 7.75 and 25°C, respectively. The sensor was used for the determination of hypoxhantine in fish meat. Results show that the fish degraded very rapidly after seven days and the hypoxanthine amount was found to increase over days of storage.

Amperometric cholesterol biosensors based on the electropolymerization of pyrrole and aniline in sulphuric Acid for the determination of cholesterol in serum.

A new amperometric cholesterol biosensor was prepared by immobilizing cholesterol oxidase by a glutaraldehyde crosslinking procedure on polypyrrole-polyaniline (ppy-pani) composite film on the surface of a platinum electrode. In order to prepare a biosensor for the determination of cholesterol, electropolymerization of pyrrole and aniline on Pt surface was performed with an electrochemical cell containing pyrrole and aniline in sulphuric acid by cyclic voltammetry between 0.0 and 0,7 V (vs.Ag/AgCl) at a scan rate of 50 mV upon Pt electrode. The amperometric determination is based on the electrochemical detection of H(2)O(2), which is generated in enzymatic reaction of cholesterol. The cholesterol determined by the oxidation of enzymatically generated H(2)O(2) at 0.7 V vs. Ag/AgCl. The optimized cholesterol oxidase biosensor displayed linear working range and a response time of 300 s. The effects of pH and temperature were investigated and optimum parameters were found to be 7.0, 25 degrees C, respectively. In addition to this, the stability and reproducibility of biosensor were tried. Operational stability of the proposed cholesterol biosensor was obtained by periodical measurements of the biosensor response. Biosensor at optimum activity conditions was used in 30 activity assays in one day to determine the operational stability. The results show that 82% of the response current was retained after 30 activity assays. The electrode was stored in a refrigerator at 4 degrees C after the measurements. The storage stability of the biosensor was determined by performing activity assays within 23 days. The results demonstrate that 60% of the response current was retained after 23 days. Preparing biosensor is used for the analysis of cholesterol in serum.

Preparation of a polypyrrole-polyvinylsulphonate composite film biosensor for determination of cholesterol based on entrapment of cholesterol oxidase.

In this paper, a novel amperometric cholesterol biosensor with immobilization of cholesterol oxidase on electrochemically polymerized polypyrrole-polyvinylsulphonate (PPy-PVS) films has been accomplished via the entrapment technique on the surface of a platinum electrode. Electropolymerization of pyrrole and polyvinylsulphonate on the Pt surface was carried out by cyclic voltammetry between -1.0 and +2.0 V (vs. Ag/AgCl) at a scan rate of 100 mV upon the Pt electrode with an electrochemical cell containing pyrrole and polyvinylsulphonate. The amperometric determination is based on the electrochemical detection of H(2)O(2) generated in the enzymatic reaction of cholesterol. Determination of cholesterol was carried out by the oxidation of enzymatically produced H(2)O(2) at 0.4 V vs. Ag/AgCl. The effects of pH and temperature were investigated and optimum parameters were found to be 7.25 and 35 °C, respectively. The storage stability and operational stability of the enzyme electrode were also studied. The results show that 32% of the response current was retained after 19 activity assays. The prepared cholesterol biosensor retained 43% of initial activity after 45 days when stored in 0.1 M phosphate buffer solution at 4 °C.

Cr(III), Fe(III) and Co(III) complexes of tetradentate (ONNO) Schiff base ligands: synthesis, characterization, properties and biological activity.

A series of metal complexes were synthesized from equimolar amounts of Schiff bases: 1,4-bis[3-(2-hydroxy-1-naphthaldimine)propyl]piperazine (bappnaf) and 1,8-bis[3-(2-hydroxy-1-naphthaldimine)-p-menthane (damnaf) with metal chlorides. All of synthesized compounds were characterized by elemental analyses, spectral (UV-vis, IR, (1)H-(13)C NMR, LC-MS) and thermal (TGA-DTA) methods, magnetic and conductance measurements. Schiff base complexes supposed in tetragonal geometry have the general formula [M(bappnaf or damnaf)]Cl.nH(2)O, where M=Cr(III), Co(III) and n=2, 3. But also Fe(III) complexes have octahedral geometry by the coordination of two water molecules and the formula is [Fe(bappnaf or damnaf)(H(2)O)(2)]Cl. The changes in the selected vibration bands in FT-IR indicate that Schiff bases behave as (ONNO) tetradentate ligands and coordinate to metal ions from two phenolic oxygen atoms and two azomethine nitrogen atoms. Conductance measurements suggest 1:1 electrolytic nature of the metal complexes. The synthesized compounds except bappnaf ligand have the antimicrobial activity against the bacteria: Escherichia coli (ATCC 11230), Yersinia enterocolitica (ATCC 1501), Bacillus magaterium (RSKK 5117), Bacillus subtilis (RSKK 244), Bacillus cereus (RSKK 863) and the fungi: Candida albicans (ATCC 10239). These results have been considerably interest in piperazine derivatives due to their significant applications in antimicrobial studies.

Immobilization of uricase upon polypyrrole-ferrocenium film.

In this study, uricase was immobilized by a glutaraldehyde/gelatine crosslinking procedure onto polypyrrole film. The K(m) value for immobilized enzyme 0.44 mM was much higher than that of the free enzyme 0.39 mM. V(max) values were 8.4 x 10(-2) mM/dak and 7.1 x 10(-2) mM/dak for free and immobilized enzyme, respectively. The optimal pH values for free and immobilized enzymes were 8.5 and 8.0, respectively. The optimum temperature for both free and immobilized uricase was 35 degrees C and 55 degrees C. The enzyme activity after storage for 7 weeks was found to be 42% and 49% of the initial activity values for free and immobilized enzymes, respectively. The amperometric current obtained after 30 measurements at a constant uric acid concentration of 5.0 x 10(-5) M was found to be 77.7% of initial activity.

An amperometric biosensor for uric acid determination prepared from uricase immobilized in polypyrrole film.

In order to prepare a biosensor for the determination of uric acid, electropolymerization of pyrrole on Pt surface was carried out with an electrochemical cell containing pyrrole, ferrocene (as a electron mediator) and tetrabutylammonium tetrafluoroborat in acetonitrile by cyclic voltammetry between 0.0 and 1.0 V (vs. Ag/AgCl) at a scan rate of 50 mV/s upon Pt electrode. Uricase was immobilized by a glutaraldehyde/gelatine croslinking procedure on to polypyrrole film after the electropolymerization processes. The response of the biosensor against uric acid was measured after 330 seconds following the application of a constant potential of +0.7 V (vs. Ag/AgCl). The resulting biosensor exhibits excellent electrocatalysis for the uric acid. The amperometric determination is based on the electrochemical detection of H2O2, which is generated in enzymatic reaction of uric acid. The sensor responds to uric acid with a detection limit of 5.0 x 10(-7) M. The sensor remains relatively stable for 5 weeks. Interference effect were investigated on the amperometric response of the biosensor. Determination of uric acid was carried out in the biological fluids by biosensor.