- Antibacterial metal complexes of o-sulfamoylbenzoic acid: Synthesis, characterization, and DFT study
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Herein, antibacterial transition metal complexes of ML2 type having o-sulfamoylbenzoic acid as ligand were synthesized from saccharin. All characterization techniques confirmed the syntheses of non-ionic transition metal MnII (3), CoII (4), NiII (5), CuII (6), and ZnII (7) complexes, where mono-anionic o-sulfamoylbenzoic acid acts as a weak field ligand. The FT-IR, elemental analysis, and magnetic susceptibility studies suggested octahedral and square pyramidal geometries depending on the nature of metal ions. Biological activity of these complexes was studied by using six bacterial strains. Interestingly, the bacterial strains Escherichia coli and Klebsiella aerogenes were inhibited to the maximum level by 6. Among aforementioned five complexes, 4 and 6 were found in crystalline form. Apart from experimental study, DFT study was also performed for entitled complexes at the M06/6-311G(d,p) level. A comparative investigation was performed for geometrical parameters and vibrational analysis, and an agreement was obtained. Natural bonding orbital investigations expressed larger value of stabilization energy 21 kcal/mol for 3, 4, and 6 while 42 kcal/mol for 5 and 7. Furthermore, global reactivity findings also disclosed higher value of hardness (2.44–3.09 eV) for entitled chromophores, hence, showed more stability. Moreover, frontier molecular orbital (FMO) findings revealed a larger band gap (4.48–6.19 eV) with higher values of LUMO found for all complexes.
- Ali, Akbar,Ashraf, Adnan,Hanif, Muhammad,Imran, Muhammad,Irfan, Ahmad,Khalid, Muhammad,Khan, Muhammad Usman,Parvez, Masood,Shafiq, Iqra,Sher, Falak,Siddiqui, Waseeq Ahmad
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- Efficient Inhibition of Human Leukocyte Elastase and Cathepsin G by Saccharin Derivatives
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A series of saccharin derivatives I has been synthesized and evaluated for their inhibitory activity toward human leukocyte elastase and cathepsin G.Most of the compounds were found to be efficient and time-dependent inhibitors of elastase.Inactivated elastase was found to regain its activity almost fully after 24 h (80-90 percent activity) and the half-lives of reactivation ranged between 12-15 h.Addition of hydroxylamine to fully-inactivated enzyme led to rapid and complete recovery of enzymatic activity.A tentative mechanism of action is proposed on the basis of biochemical and model studies.
- Groutas, William C.,Houser-Archield, Nadene,Chong, Lee S.,Venkataraman, Radhika,Epp, Jeffrey B.,et al.
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p. 3178 - 3181
(2007/10/02)
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- Sulfamylbenzoic acids
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Certain mono- and disubstituted-5-sulfamylbenzoic acids, many of which are novel, and their use in lowering blood lipid levels in mammals.
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