No abstract

In this study, hybrid analogs of benzimidazole containing a thiazole moiety (1–17) were afforded and then tested for their ability to inhibit α-amylase and α-glucosidase when compared to acarbose as a standard drug. The recently available analogs showed a wide variety of inhibitory potentials that ranged between 1.31 ± 0.05 and 38.60 ± 0.70 µM (against α-amylase) and between 2.71 ± 0.10 and 42.31 ± 0.70 µM (against α-glucosidase) under the positive control of acarbose (IC50 = 10.30 ± 0.20 µM against α-amylase) (IC50 = 9.80 ± 0.20µM against α-glucosidase). A structure–activity relationship (SAR) study was carried out for all analogs based on substitution patterns around both rings B and C respectively. It was concluded from the SAR study that analogs bearing either substituent(s) of smaller size (−F and Cl) or substituent(s) capable of forming hydrogen bonding (−OH) with the catalytic residues of targeted enzymes enhanced the inhibitory potentials. Therefore, analogs 2 (bearing meta-fluoro substitution), 3 (having para-fluoro substitution) and 4 (with ortho-fluoro group) showed enhanced potency when evaluated against standard acarbose drug with IC50 values of 4.10 ± 0.10, 1.30 ± 0.05 and 1.90 ± 0.10 (against α-amylase) and 5.60 ± 0.10, 2.70 ± 0.10 and 2.90 ± 0.10 µM (against α-glucosidase), correspondingly. On the other hand, analogs bearing substituent(s) of either a bulky nature (−Br) or that are incapable of forming hydrogen bonds (−CH3) were found to lower the inhibitory potentials. In order to investigate the binding sites for synthetic analogs and how they interact with the active areas of both targeted enzymes, molecular docking studies were also conducted on the potent analogs. The results showed that these analogs adopted many important interactions with the active areas of enzymes. The precise structure of the newly synthesized compounds was confirmed using several spectroscopic techniques as NMR and HREI-MS.

This work successfully created a polypyrrole-polyethyleneimine (PPy-PEI) nano adsorbent for the elimination of the lead ion Pb2+ from an aqueous solution. An efficient conducting polymer-based adsorbent called as was created using ammonium persulfate (NH4)2S2O8 as an oxidant (PPy-PEI). The PEI hyper-branched polymer with terminal amino groups was added to the PPy adsorbent to offer heavy metals more effective chelating sites. Pb2+ removal from aqueous solution using polyethyleneimine micro adsorbent was successfully accomplished using a batch equilibrium technique (PPy-PEI). The generated water-insoluble polymer nanoadsorbent had enough nitrogen atoms; therefore, an effort was made to link PEI, a water-soluble PPy, with PPy, a conjugated polymer, for lead ion adsorption from an aqueous solution. The generated PPy-PEI nanoadsorbents were discovered to have average particle sizes of 18–34 nm and a Brunauer-Emmet-Teller surface area of 17 m2/g, respectively. The thermal behavior of the composites was investigated using thermo gravimetric and differential scanning calorimetric methods. The lead ion adsorption efficacy of pure polypyrrole was found to be 38%; however, a batch equilibrium technique employing nanoadsorbent revealed with the maximum adsorption capacity of 75.60 mg g−1. At pH 10 and 30 min of contact time at 50 °C, 0.2 g of adsorption was shown to be the ideal dosage. X-ray diffraction analysis, energy-dispersive ray spectroscopy, and Fourier transform infrared ray spectrum support the lead ion adsorption by PPy-PEI nanoadsorbents. The cauli-like structure was visible using field emission scanning electron microscopy. Studying the thermodynamic showed that the adsorption was endothermic as illustrated from the positive value of value of ΔH° is 1.439 kJ/mol which indicates that the uptake of Pb2+onto nanoadsorbent PPy-PEI could be attributed to a physical adsorption process. According to the values of ΔG°, the adsorption process was spontaneous at all selected temperatures. The positive value of ΔS° value (43.52 j/mol) suggested an increase in the randomness at the solid/solution interface during the adsorption process. The adsorption data meet the pseudo-second-order kinetic model and suited the Langumuir isothermal model effectively.

Twenty-four analogs based on triazinoindole bearing benzimidazole/benzoxazole moieties (1–25) were synthesized. Utilizing a variety of spectroscopic methods, including 1H-, 13C-NMR, and HREI-MS, the newly afforded compounds (1–25) were analyzed. The synthesized analogs were tested against urease enzyme (in vitro) as compared to the standard thiourea drug. All triazinoindole-based benzimidazole/benzoxazole analogs (1–25) exhibited moderate to excellent inhibition profiles, having IC50 values of 0.20 ± 0.01 to 36.20 ± 0.70 μM when evaluated under the positive control of thiourea as a standard drug. To better understand the structure–activity relationship, the synthesized compounds were split into two groups, “A” and “B.” Among category “A” analogs, analogs 8 (bearing tri-hydroxy substitutions at the 2,4,6-position of aryl ring C) and 5 (bearing di-hydroxy substitutions at the 3,4-position of aryl ring C) emerged as the most potent inhibitors of urease enzyme and displayed many times more potency than a standard thiourea drug. Besides that, analog 22 (which holds di-hydroxy substitutions at the 2,3-position of the aryl ring) and analog 23 (bearing ortho-fluoro substitution) showed ten-fold-enhanced inhibitory potential compared to standard thiourea among category “B” analogs. Molecular docking studies on the active analogs of each category were performed; the results obtained revealed that the presence of hydroxy and fluoro-substitutions on different positions of aryl ring C play a pivotal role in binding interactions with the active site of the targeted urease enzyme.