Abstract:The inhibition effect of meso-tetraphenyl-porphyrin (TPPH2), meso-tetra4-methophenyl-porphyrin TPPH2(p-Me), and meso-tetra4-actophenyl-porphyrin (TAcPPH2) on the corrosion of XC52 mild steel in aerated 0.5 M aqueous sulfuric acid solution was studied by potentiodynamic polarization experiments and quantum chemical calculations. Results from potentiodynamic polarization showed that inhibition efficiency of three compounds increased upon increasing of the inhibitor concentration and they are acting as mixed type… Show more
“…Meso-tetramethophenyl-porphyrin and meso-tetrabiphenyl-porphyrin represent macrocyclic aromatic compounds characterized by an 18π electron structure, composed of four pyrrole subunits interconnected through methine bridges. These compounds exhibit noteworthy electron mobility within the ring, rendering 2 them suitable for diverse applications (Meraghni et al, 2023), including electrochemistry and catalysis (Zuriaga-Monroy et al, 2016), photomedicine (Boutarfaia et al, 2020), and photosynthesis (Zaiz et al, 2012). The nitrogen atoms in these compounds possess the ability to engage in reactions with metal ions, forming stable metalloporphyrin complexes, with transition metal ion complexes being the most extensively studied (Thompson et al, 2018).…”
The investigation employed cyclic voltammetry (CV) assays to assess the scavenging efficacy of two recently developed compounds, namely meso-tetramethophenyl-porphyrin TPPH2(o-methyl) and meso-tetrabiphenyl-porphyrin (TbiPPH2), against the superoxide anion radical ( ). The IC50 values derived from the CV assays indicated significant scavenging activity for both compounds, with TbPPH2 exhibiting superior potency (85.79 ± 0.11 µg ml-1) compared to the standard antioxidant alpha-tocopherol (353.27 ± 3.21 µg ml-1). Additionally, molecular docking simulations elucidated the interaction of the investigated compounds with specific amino acid residues of glutathione reductase through hydrogen bonding and hydrophobic interactions. The in vitro and in silico results were concordant, highlighting TbiPPH2 as the least active compound against glutathione reductase, boasting the highest inhibitory concentration of 0.63 μM and the lowest docking score of -35.36 kJ mol-1, thus positioning it as a promising candidate for antioxidant applications.
“…Meso-tetramethophenyl-porphyrin and meso-tetrabiphenyl-porphyrin represent macrocyclic aromatic compounds characterized by an 18π electron structure, composed of four pyrrole subunits interconnected through methine bridges. These compounds exhibit noteworthy electron mobility within the ring, rendering 2 them suitable for diverse applications (Meraghni et al, 2023), including electrochemistry and catalysis (Zuriaga-Monroy et al, 2016), photomedicine (Boutarfaia et al, 2020), and photosynthesis (Zaiz et al, 2012). The nitrogen atoms in these compounds possess the ability to engage in reactions with metal ions, forming stable metalloporphyrin complexes, with transition metal ion complexes being the most extensively studied (Thompson et al, 2018).…”
The investigation employed cyclic voltammetry (CV) assays to assess the scavenging efficacy of two recently developed compounds, namely meso-tetramethophenyl-porphyrin TPPH2(o-methyl) and meso-tetrabiphenyl-porphyrin (TbiPPH2), against the superoxide anion radical ( ). The IC50 values derived from the CV assays indicated significant scavenging activity for both compounds, with TbPPH2 exhibiting superior potency (85.79 ± 0.11 µg ml-1) compared to the standard antioxidant alpha-tocopherol (353.27 ± 3.21 µg ml-1). Additionally, molecular docking simulations elucidated the interaction of the investigated compounds with specific amino acid residues of glutathione reductase through hydrogen bonding and hydrophobic interactions. The in vitro and in silico results were concordant, highlighting TbiPPH2 as the least active compound against glutathione reductase, boasting the highest inhibitory concentration of 0.63 μM and the lowest docking score of -35.36 kJ mol-1, thus positioning it as a promising candidate for antioxidant applications.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.