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14 Αποτελέσματα
Designing and characterization of copper (II) ion-imprinted adsorbent based on isatin functionalized chitosan.
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An isatin functionalized chitosan derived ion-imprinted adsorbent (Cu-CIS) was designed by tailoring Cu(II) ions imprinted cavities within the modified polysaccharide network matrix that are able to capture Cu(II) ions selectively in aqueous solution. The chelating power of chitosan toward the
Inhibition of monoamine oxidase by selected C5- and C6-substituted isatin analogues.
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Previous studies have shown that (E)-5-styrylisatin and (E)-6-styrylisatin are reversible inhibitors of human monoamine oxidase (MAO) A and B. Both homologues are reported to exhibit selective binding to the MAO-B isoform with (E)-5-styrylisatin being the most potent inhibitor. To further
Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition, herbicidal activity, and computational studies of isatin derivatives.
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Acetohydroxyacid synthase (AHAS) catalyzes the first common step in the biosynthesis of the branched-chain amino acids. As a result of its metabolic importance in plants, it is a target for many commercial herbicides. Virtual screening analysis inspired the evaluation of 19 commercially available
Differential binding modes of anti-cancer, anti-HIV drugs belonging to isatin family with a model transport protein: a joint refinement from spectroscopic and molecular modeling approaches.
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The present contribution reports a detailed characterization of the binding interaction of two potential anticancer, anti-HIV drugs isatin (IST) and 1-methylisatin (MI) with model transport protein Bovine Serum Albumin (BSA). Thermodynamic parameters e.g., ΔH, ΔS and ΔG for the binding phenomenon
Structure and mechanism of monoamine oxidase.
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Monoamine oxidases A and B (MAO A and MAO B) are mitochondrial outer membrane-bound flavoproteins that catalyze the oxidative deamination of neurotransmitters and biogenic amines. A number of mechanism-based inhibitors (MAOI's) have been developed for clinical use as antidepressants and as
Inhibition of monoamine oxidase by (E)-styrylisatin analogues.
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Previous studies have shown that (E)-8-(3-chlorostyryl)caffeine (CSC) is a specific reversible inhibitor of human monoamine oxidase B (MAO-B) and does not bind to human MAO-A. Since the small molecule isatin is a natural reversible inhibitor of both MAO-B and MAO-A, (E)-5-styrylisatin and
Computer visualisation of the active site of monoamine oxidase-A by means of selective inhibitors.
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Computer visualisation of the active site of monoamine oxidase (MAO) is based on an assumption that the specific and reversible interaction of a ligand (substrate or inhibitor) with the substrate-binding region of the active site requires shape complementarity. The size of the ligand must allow its
Efficient synthesis of new antiproliferative steroidal hybrids using the molecular hybridization approach.
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A series of steroidal hybrids with different terminal bioactive scaffolds were synthesized using the molecular hybridization approach and further evaluated for their antiproliferative activity against several cancer cell lines of different origins using the MTT assay. The preliminary results
Inhibition of monoamine oxidase by C5-substituted phthalimide analogues.
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Literature reports that isatin as well as C5- and C6-substituted isatin analogues are reversible inhibitors of human monoamine oxidase (MAO) A and B. In general, C5- and C6-substitution of isatin leads to enhanced binding affinity to both MAO isozymes compared to isatin and in most instances result
A review on phytochemical, pharmacological, and pharmacognostical profile of Wrightia tinctoria: Adulterant of kurchi.
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Wrightia tinctoria R. Br. belongs to family Apocynaceae commonly called as Sweet Indrajao, Pala Indigo Plant, Dyer's Oleander. "Jaundice curative tree" in south India. Sweet Indrajao is a small, deciduous tree with a light gray, scaly smooth bark. Native to India and Burma, Wrightia is named after a
Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors.
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Several reversible inhibitors selective for human monoamine oxidase B (MAO B) that do not inhibit MAO A have been described in the literature. The following compounds: 8-(3-chlorostyryl)caffeine, 1,4-diphenyl-2-butene, and trans,trans-farnesol are shown to inhibit competitively human, horse, rat,
The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution.
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Monoamine oxidase from Aspergillus niger (MAO-N) is a flavoenzyme that catalyses the oxidative deamination of primary amines. MAO-N has been used as the starting model for a series of directed evolution experiments, resulting in mutants of improved activity and broader substrate specificity,
Structure of the human mitochondrial monoamine oxidase B: new chemical implications for neuroprotectant drug design.
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Monoamine oxidase B (MAO-B) is an outer mitochondrial membrane-bound flavoenzyme that is a well-known target for antidepressant and neuroprotective drugs. The 3A resolution structure of recombinant human MAO-B originally determined was of the enzyme complexed with pargyline, an irreversible
Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures.
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Monoamine oxidase B (MAO-B) is an outer mitochondrial membrane-bound enzyme that catalyzes the oxidative deamination of arylalkylamine neurotransmitters and has been a target for a number of clinically used drug inhibitors. The 1.7-A structure of the reversible isatin-MAO-B complex has been
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