Ipomotaosides A−D, Resin Glycosides from the Aerial Parts ofIpomoea batatasand Their Inhibitory Activity against COX-1 and COX-2

2010 ◽  
Vol 73 (11) ◽  
pp. 1763-1766 ◽  
Author(s):  
Kazuko Yoshikawa ◽  
Chiho Yagi ◽  
Hiroshi Hama ◽  
Masami Tanaka ◽  
Shigenobu Arihara ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Aerial Parts ◽  
Cox 2 ◽  
Cox 1

scholarly journals Health-Beneficial Phenolic Aldehyde inAntigonon leptopusTea

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Vanisree Mulabagal ◽  
Ruby L. Alexander-Lindo ◽  
David L. DeWitt ◽  
Muraleedharan G. Nair
Keyword(s):  
Lipid Peroxidation ◽  
Pain Relief ◽  
Inhibitory Activity ◽  
Inhibitory Concentration ◽  
Aerial Parts ◽  
Bioassay Guided Fractionation ◽  
Inhibitory Activities ◽  
Cox 2 ◽  
Dried Extract ◽  
Cox 1

Tea prepared from the aerial parts ofAntigonon leptopusis used as a remedy for cold and pain relief in many countries. In this study,A. leptopustea, prepared from the dried aerial parts, was evaluated for lipid peroxidation (LPO) and cyclooxygenase (COX-1 and COX-2) enzyme inhibitory activities. The tea as a dried extract inhibited LPO, COX-1 and COX-2 enzymes by 78%, 38% and 89%, respectively, at 100 g/mL. Bioassay-guided fractionation of the extract yielded a selective COX-2 enzyme inhibitory phenolic aldehyde, 2,3,4-trihydroxy benzaldehyde. Also, it showed LPO inhibitory activity by 68.3% at 6.25 g/mL. Therefore, we have studied other hydroxy benzaldehydes and their methoxy analogs for LPO, COX-1 and COX-2 enzymes inhibitory activities and found that compound1gave the highest COX-2 enzyme inhibitory activity as indicated by a 50% inhibitory concentration (IC50) at 9.7 g/mL. The analogs showed only marginal LPO activity at 6.25 g/mL. The hydroxy analogs6,7and9showed 55%, 61% and 43% of COX-2 inhibition at 100 g/mL. However, hydroxy benzaldehydes3and12showed selective COX-1 inhibition while compounds4and10gave little or no COX-2 enzyme inhibition at 100 g/mL. At the same concentration, compounds14,21and22inhibited COX-1 by 83, 85 and 70%, respectively. Similarly, compounds18,19and23inhibited COX-2 by 68%, 72% and 70%, at 100 g/mL. This is the first report on the isolation of compound1fromA. leptopustea with selective COX-2 enzyme and LPO inhibitory activities.

New indomethacin analogs as selective COX‐2 inhibitors: Synthesis, COX‐1/2 inhibitory activity, anti‐inflammatory, ulcerogenicity, histopathological, and docking studies

2020 ◽  
Author(s):  
Khaled R. A. Abdellatif ◽  
Eman K. A. Abdelall ◽  
Heba A. H. Elshemy ◽  
El‐Shaymaa El‐Nahass ◽  
Maha M. Abdel‐Fattah ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Docking Studies ◽  
Cox 2 ◽  
Anti Inflammatory ◽  
Cox 2 Inhibitors ◽  
Cox 1

In vitro COX-1, COX-2 and 5-LOX inhibitory activity of plant family Ranunculaceae

Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
J Malik ◽  
P Landa ◽  
Z Kutil ◽  
P Marsik ◽  
L Kokoska
Keyword(s):  
Inhibitory Activity ◽  
Plant Family ◽  
Cox 2 ◽  
Cox 1

scholarly journals Kinetic basis for selective inhibition of cyclo-oxygenases

1999 ◽  
Vol 339 (3) ◽  
pp. 607-614 ◽  
Author(s):  
James K. GIERSE ◽  
Carol M. KOBOLDT ◽  
Mark C. WALKER ◽  
Karen SEIBERT ◽  
Peter C. ISAKSON
Keyword(s):  
Inhibitory Activity ◽  
Tight Binding ◽  
Selective Inhibition ◽  
Time Dependent ◽  
Experimental Conditions ◽  
Kinetic Behaviour ◽  
Competitive Kinetics ◽  
Binding Time ◽  
Cox 2 ◽  
Cox 1

Non-steroidal anti-inflammatory drugs (NSAIDs) inhibit the formation of prostaglandins by cyclo-oxygenases (COX). The discovery of a second COX isoform (COX-2) associated with inflammation led to agents that selectively inhibit COX-2, e.g. celecoxib. We evaluated the kinetics of inhibition of celecoxib and several NSAIDs. Celecoxib displays classic competitive kinetics on COX-1 (Ki = 10-16 μM). An initial competitive interaction with COX-2 can also be discerned with celecoxib (Ki = 11-15 μM), followed by a time-dependent interaction leading to potent inhibition, characterized as inactivation (Kinact = 0.03-0.5 s-1). Half-maximal inhibition (IC50) using end-point assays reflects the competitive component on COX-1 (IC50 = 4-19 μM) and the inactivation component on COX-2 (IC50 = 0.003-0.006 μM). NSAIDs exhibit four distinct modes of COX inhibition based on kinetic behaviour: (1) competitive, e.g. ibuprofen; (2) weak binding, time-dependent, e.g. naproxen, oxicams; (3) tight binding, time-dependent, e.g. indomethacin; (4) covalent, e.g. aspirin. In addition, most NSAIDs display different kinetic behaviour for each isoform. Weakly binding inhibitors show variable behaviour in enzyme assays, with apparent inhibitory activity being markedly influenced by experimental conditions; determination of kinetic constants with this class is unreliable and IC50 values are strongly dependent on assay conditions. Although IC50 determinations are useful for structure/activity analyses, the complex and distinct mechanisms of enzyme inhibition of each COX isoform by the NSAIDs renders comparison of inhibitory activity on COX-1 and COX-2 using IC50 ratios of questionable validity.

Flavonoids and Stilbenoids with COX-1 and COX-2 Inhibitory Activity fromDracaena loureiri

Planta Medica ◽  
2002 ◽  
Vol 68 (9) ◽  
pp. 841-843 ◽  
Author(s):  
Kittisak Likhitwitayawuid ◽  
Kanokporn Sawasdee ◽  
Kanyawim Kirtikara
Keyword(s):  
Inhibitory Activity ◽  
Cox 2 ◽  
Cox 1

In vitro COX-1, COX-2 and 5-LOX inhibitory activity of rose hips (Rosae pseudofructus sine fructibus)

Planta Medica ◽  
2007 ◽  
Vol 73 (09) ◽  
Author(s):  
EM Wenzig ◽  
U Widowitz ◽  
O Kunert ◽  
R Bauer ◽  
S Chrubasik
Keyword(s):  
Inhibitory Activity ◽  
Cox 2 ◽  
Cox 1

scholarly journals Characteristics of New Peptides GQLGEHGGAGMG, GEHGGAGMGGGQFQPV, EQGFLPGPEESGR, RLARAGLAQ, YGNPVGGVGH, and GNPVGGVGHGTTGT as Inhibitors of Enzymes Involved in Metabolic Syndrome and Antimicrobial Potential

Molecules ◽  
2020 ◽  
Vol 25 (11) ◽  
pp. 2492 ◽  
Author(s):  
Urszula Złotek ◽  
Anna Jakubczyk ◽  
Kamila Rybczyńska-Tkaczyk ◽  
Paula Ćwiek ◽  
Barbara Baraniak ◽  
...  
Keyword(s):  
Metabolic Syndrome ◽  
Antimicrobial Activity ◽  
Inhibitory Activity ◽  
Synthetic Peptides ◽  
Cytotoxic Effect ◽  
Inhibitory Effect ◽  
Converting Enzyme ◽  
Cox 2 ◽  
Enzyme I ◽  
Cox 1

The aim of this study was to determine the cytotoxic properties, influence on enzyme activity involved in metabolic syndrome, and antimicrobial activity of synthetic peptides with GQLGEHGGAGMG, GEHGGAGMGGGQFQPV, EQGFLPGPEESGR, RLARAGLAQ, YGNPVGGVGH, and GNPVGGVGHGTTGT sequences. Peptides have no cytotoxic effect on cells. The highest inhibitory effect on angiotensin converting enzyme I was noted for peptide GT-14 (IC50 = 525.63 µg/mL). None of the tested peptides had an influence on α-glucosidase. The highest α-amylase and lipase inhibitory activity was noted for GG-12 (IC50 = 56.72 and 60.62 µg/mL, respectively). The highest lipoxidase inhibitory activity was determined for peptide ER-13 (IC50 = 84.35 µg/mL). Peptide RQ-9 was characterized by the highest COX inhibitory activity (0.31 and 4.77 µg/mL for COX-1 and COX-2, respectively). Only peptide RQ-9 inhibited S. enteritidis ATCC 4931 growth (42–48%) in all tested concentrations (15.62–250 mg/mL).

scholarly journals DESIGN, SYNTHESIS AND BIOLOGICAL SCREENING OF AMINOACETYLENIC TETRAHYDROPHTHALIMIDE ANALOGUES AS NOVEL CYCLOOXYGENASE (COX) INHIBITORS

2017 ◽  
Vol 9 (2) ◽  
pp. 160
Author(s):  
Ahmed Basim ◽  
Zuhair A. Muhi Eldeen ◽  
Elham N. Al-kaissi ◽  
Ghadeer Suaifan ◽  
Mohammad A. Ghattas ◽  
...  
Keyword(s):  
Elemental Analysis ◽  
Inhibitory Activity ◽  
Aryl Group ◽  
Design Synthesis ◽  
Cox Inhibitors ◽  
H Nmr ◽  
Phthalimide Derivative ◽  
Cox 2 ◽  
Cox 1 ◽  
C Nmr

<p><strong>Objective: </strong>To design and synthesise a new amino acetylenic tetrahydro phthalimide derivative and investigate their selective inhibitory activity to COXs.</p><p><strong>Methods: </strong>Aminoacetylenic tetrahydro phthalimide derivatives were synthesised by alkylation of tetrahydro phthalimide with propargyl bromide afforded 2-(prop-2-yn-1-yl)-2,3,3a,4,7,7a-hexahydro-1H-isoindole-1,3-dione. The alkylated tetrahydro phthalimide was subjected to Mannich reaction afforded the desired amino acetylenic tetra phthalimide derivatives (AZ 1-6). The elemental analysis was indicated by the EuroEA elemental analyzer and biological characterization was via IR, <sup>1</sup>H-NMR, [13]C-NMR, DSC was determined with the aid of Bruker FT-IR and Varian 300 MHz spectrometer and DMSO-d<sub>6</sub> as a solvent, molecular docking was done using the Autodock Tool software (version 4.2). ChemBioDraw was used in the drawing of our schemes.</p><p><strong>Results</strong>:<strong> </strong>The IR, <sup>1</sup>H-NMR, <sup>13</sup>C-NMR, DSC and elemental analysis were consistent with the assigned structures. The designers of the compounds as COXs inhibitor activity were based on the nationalisation of the important criteria that provide effective inhibitory binding with COXs–receptor. The results indicated that the synthesised compounds (AZ1-6) showed a close similarity in the binding affinity to both COXs and may be more specific to COX-1. AZ-5 showed the highest % of inhibition for COX-1 even better than aspirin. Which may suggest that the aryl group is required for COX-2 inhibition.</p><p><strong>Conclusion: </strong>For the first time, we indicate the requirement of aromaticity in COX-2 structural inhibitory activity. </p>

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