Mild steel (MS) corrosion is a worldwide issue that greatly affects the industrial and natural environment. To extend the lifespan of appliances, the control of MS corrosion is necessary. To shield MS from corrosion, specifically from acidic conditions, one of the practical and finest approaches is the application of inhibitors. Triazole derivatives are eco-friendly corrosion inhibitors (CIs) having inconsequential toxicities, excellent inhibition efficiencies (IEs) against corrosion of MS, and extremely high cost-effectiveness. This critical review discusses the general effect of temperature, concentration, time after the application of CI, and type of acid on the IE of triazole derivatives. Further, the review provides an adequate amount of information about the features of excellent CIs; a summary of the reported properties of triazole-based inhibitors, CIs in industries, and current requirements of industries; and recommendations and implications for researchers to improve IE. Additionally, the review also illustrates the mechanisms of action and the IEs, which are evaluated from potentiodynamic polarization parameters, in various acidic media and concentrations of triazole inhibitors. By IE correlation with numerous concentrations and acidic conditions, this review is advantageous and helpful for synthetic chemists to expand the diversity and complexity of a class of triazole derivatives by synthesizing new triazole derivatives.

A series of symmetrical salicylaldehyde-bishydrazine azo molecules, 5a–5h, have been synthesized, characterized by ¹H-NMR and ¹³C-NMR, and evaluated for their in vitro α-glucosidase and α-amylase inhibitory activities. All the synthesized compounds efficiently inhibited both enzymes. Compound 5g was the most potent derivative in the series, and powerfully inhibited both α-glucosidase and α-amylase. The IC₅₀ of 5g against α-glucosidase was 0.35917 ± 0.0189 µM (standard acarbose IC₅₀ = 6.109 ± 0.329 µM), and the IC₅₀ value of 5g against α-amylase was 0.4379 ± 0.0423 µM (standard acarbose IC₅₀ = 33.178 ± 2.392 µM). The Lineweaver-Burk plot indicated that compound 5g is a competitive inhibitor of α-glucosidase. The binding interactions of the most active analogues were confirmed through molecular docking studies. Docking studies showed that 5g interacts with the residues Trp690, Asp548, Arg425, and Glu426, which form hydrogen bonds to 5g with distances of 2.05, 2.20, 2.10 and 2.18 Å, respectively. All compounds showed high mutagenic and tumorigenic behaviors, and only 5e showed irritant properties. In addition, all the derivatives showed good antioxidant activities. The pharmacokinetic evaluation also revealed promising results

Sulfonamide derivatives serve as an important building blocks in the drug design discovery and development (4D) process. Ciprofloxacin-, sulfadiazine- and amantadine-based sulfonamides were synthesized as potent inhibitors of jack bean urease and free radical scavengers. Molecular diversity was explored and electronic factors were also examined. All 24 synthesized compounds exhibited excellent potential against urease enzyme. Compound 3e (IC₅₀ = 0.081 ± 0.003 µM), 6a (IC₅₀ = 0.0022 ± 0.0002 µM), 9e (IC₅₀ = 0.0250 ± 0.0007 µM) and 12d (IC₅₀ = 0.0266 ± 0.0021 µM) were found to be the lead compounds compared to standard (thiourea, IC₅₀ = 17.814 ± 0.096 µM). Molecular docking studies were performed to delineate the binding affinity of the molecules and a kinetic mechanism of enzyme inhibition was propounded. Compounds 3e, 6a and 12d exhibited a mixed type of inhibition, while derivative 9e revealed a non-competitive mode of inhibition. Compounds 12a, 12b, 12d, 12e and 12f showed excellent radical scavenging potency in comparison to the reference drug vitamin C.