Identification of Novel Urease Inhibitors by High-Throughput Virtual and in Vitro Screening

Abid, Obaid‐ur‐Rahman; Babar, Tariq Mahmood; Ali, Farukh Iftakhar; Ahmed, Sajjad; Wadood, Abdul; Rama, Nasim Hasan; Uddin, Reaz; Ul-Haq, Zaheer; Khan, Ajmal; Choudhary, M. Iqbal

doi:10.1021/ml100068u

Cited by 78 publications

(38 citation statements)

References 17 publications

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“…The assay measurements were carried out using a micro-plate reader (OptiMax, Tunable Micro plate Reader; wavelength range 340-850 nm for 96-well plates). The reaction rates of immobilized enzyme were compared with its free counterpart, and the percentage inhibition was calculated using the formula 100 − (Abs testwell /Abs control )×100 [58], where Abs testwell is the absorbance of the well being tested and Abs control the absorbance of the control sample.…”

Section: Enzyme Activity Measurementsmentioning

confidence: 99%

Acetylcholinesterase immobilization and characterization, and comparison of the activity of the porous silicon-immobilized enzyme with its free counterpart

et al. 2016

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SynopsisA successful prescription is presented for acetylcholinesterase physically adsorbed on to a mesoporous silicon surface, with a promising hydrolytic response towards acetylthiocholine iodide. The catalytic behaviour of the immobilized enzyme was assessed by spectrophotometric bioassay using neostigmine methyl sulfate as a standard acetycholinesterase inhibitor. The surface modification was studied through field emission SEM, Fourier transform IR spectroscopy, energy-dispersive X-ray spectroscopy, cathode luminescence and X-ray photoelectron spectroscopy analysis, photoluminescence measurement and spectrophotometric bioassay. The porous silicon-immobilized enzyme not only yielded greater enzyme stability, but also significantly improved the native photoluminescence at room temperature of the bare porous silicon architecture. The results indicated the promising catalytic behaviour of immobilized enzyme compared with that of its free counterpart, with a greater stability, and that it aided reusability and easy separation from the reaction mixture. The porous silicon-immobilized enzyme was found to retain 50 % of its activity, promising thermal stability up to 90 • C, reusability for up to three cycles, pH stability over a broad pH of 4-9 and a shelf-life of 44 days, with an optimal hydrolytic response towards acetylthiocholine iodide at variable drug concentrations. On the basis of these findings, it was believed that the porous silicon-immobilized enzyme could be exploited as a reusable biocatalyst and for screening of acetylcholinesterase inhibitors from crude plant extracts and synthesized organic compounds. Moreover, the immobilized enzyme could offer a great deal as a viable biocatalyst in bioprocessing for the chemical and pharmaceutical industries, and bioremediation to enhance productivity and robustness.

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Section: Enzyme Activity Measurementsmentioning

confidence: 99%

Acetylcholinesterase immobilization and characterization, and comparison of the activity of the porous silicon-immobilized enzyme with its free counterpart

et al. 2016

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“…Urease produced by Helicobactor pylori is one of the major causes of the pathogenesis of peptic, and gastric ulcers, as well as related cancers. The discovery and development of new protein glycation and enzymes inhibitors are important for the treatment of the related diseases [7][8][9][10]. The first bioassay-guided isolation and bioactivity evaluation of P. cooperi is reported here.…”

Section: Introductionmentioning

confidence: 99%

New antiglycation and enzyme inhibitors from Parmotrema cooperi

et al. 2011

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Lichens are unique individuals which have been widely used in traditional medicines. This study was focused on the bioassayguided phytochemical investigation, and bioactivity evaluation on a lichens species, Parmotrema cooperi. This first bioassaydirected chemical study on P. cooperi has led to the isolation of ethyl heamatomate (1), atraric acid (2), ethyl orsellinate (3), orsellinic acid (4), lecanoric acid (5), gyrophoric acid (6), and licanorin (7). The structures of 17 were mainly elucidated from spectroscopic methods including 1D, and 2D NMR spectroscopy, and mass spectrometry. These compounds were evaluated for their antiglycation, urease, α-chymotrypsin, and β-glucoronidase inhibitory activities. Few of the phenolic compounds showed significant, while most of them showed good inhibition of protein glycation, and urease activities.lichen, Parmotrema cooperi, ethyl heamatomate, atraric acid, urease inhibition, antiglycation

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“…Thus, the hydrophobic portion of the compounds may be engulfed in this cavity and have a hydrophobic interaction. 121 Zaheer-ul-Haq et al 122 performed a COMFA study on a series of bis-coumarine analogues (4) as urease inhibitors in which the COMFA electrostatic plots ( Figure 10) indicated the favorable and unfavorable electrostatic fields. In this figure, the red contours indicated the regions of the compounds that can interact with the Ni 2+ ions, and, as can be seen, these regions cover both hydroxyl moieties and both lactones moieties.…”

Section: Urease Inhibitionmentioning

confidence: 99%

QSAR Studies on Hydroxamic Acids: A Fascinating Family of Chemicals with a Wide Spectrum of Activities

Gupta

2015

Chem. Rev.

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Identification of Novel Urease Inhibitors by High-Throughput Virtual and in Vitro Screening

Cited by 78 publications

References 17 publications

Acetylcholinesterase immobilization and characterization, and comparison of the activity of the porous silicon-immobilized enzyme with its free counterpart

Acetylcholinesterase immobilization and characterization, and comparison of the activity of the porous silicon-immobilized enzyme with its free counterpart

New antiglycation and enzyme inhibitors from Parmotrema cooperi

QSAR Studies on Hydroxamic Acids: A Fascinating Family of Chemicals with a Wide Spectrum of Activities

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