curcumin has been researched along with coumarin* in 7 studies
1 review(s) available for curcumin and coumarin
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Hybrid
The growing interest in anticancer hybrids in the last few years has resulted in a great number of reports on hybrid design, synthesis and bioevaluation. Many novel multi-target-directed drug candidates were synthesized, and their biological activities were evaluated. For the design of anticancer hybrid compounds, the molecules of stilbenes, aromatic quinones, and heterocycles (benzimidazole, imidazole, pyrimidine, pyridine, pyrazole, quinoline, quinazoline) were applied. A distinct group of hybrids comprises the molecules built with natural compounds: Resveratrol, curcumin, coumarin, and oleanolic acid. In this review, we present the studies on bioactive hybrid molecules of a well-known tubulin polymerization inhibitor, combretastatin A-4 and its analogs with other pharmacologically active entities. The mechanism of anticancer activity of selected hybrids is discussed considering the structure-activity relationship. Topics: Antineoplastic Agents, Phytogenic; Chemistry, Pharmaceutical; Coumarins; Curcumin; Humans; Oleanolic Acid; Resveratrol; Stilbenes; Structure-Activity Relationship | 2019 |
6 other study(ies) available for curcumin and coumarin
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Curcumin-Coumarin Hybrid Analogues as Multitarget Agents in Neurodegenerative Disorders.
Neurodegenerative diseases have a complex nature which highlights the need for multitarget ligands to address the complementary pathways involved in these diseases. Over the last decade, many innovative curcumin-based compounds have been designed and synthesized, searching for new derivatives having anti-amyloidogenic, inhibitory of tau formation, as well as anti-neuroinflammation, antioxidative, and AChE inhibitory activities. Regarding our experience studying 3-substituted coumarins with interesting properties for neurodegenerative diseases, our aim was to synthesize a new series of curcumin-coumarin hybrid analogues and evaluate their activity. Most of the 3-(7-phenyl-3,5-dioxohepta-1,6-dien-1-yl)coumarin derivatives Topics: Acetylcholinesterase; Animals; Antioxidants; Biphenyl Compounds; Butyrylcholinesterase; Cell Line, Tumor; Cell Survival; Cholinesterase Inhibitors; Coumarins; Curcumin; GPI-Linked Proteins; Humans; Hydrogen Peroxide; Monoamine Oxidase; Monoamine Oxidase Inhibitors; Motor Cortex; Nanoparticles; Neurons; Neuroprotective Agents; Picrates; Primary Cell Culture; Rats; Structure-Activity Relationship | 2021 |
New coumarin-benzotriazole based hybrid molecules as inhibitors of acetylcholinesterase and amyloid aggregation.
A novel series of triazole tethered coumarin-benzotriazole hybrids based on donepezil skeleton has been designed and synthesized as multifunctional agents for the treatment of Alzheimer's disease (AD). Among the synthesized compounds 13b showed most potent acetylcholinesterase (AChE) inhibition (IC Topics: Acetylcholinesterase; Alzheimer Disease; Amyloid beta-Peptides; Cell Line, Tumor; Cholinesterase Inhibitors; Coumarins; Dose-Response Relationship, Drug; Humans; Molecular Structure; Peptide Fragments; Protein Aggregates; Protein Aggregation, Pathological; Structure-Activity Relationship; Triazoles | 2020 |
Sortase A-Inhibitory Coumarins from the Folk Medicinal Plant
Thirteen coumarins ( Topics: Aminoacyltransferases; Bacterial Proteins; Coumarins; Cysteine Endopeptidases; Fibrinogen; Fibronectins; Gram-Positive Bacteria; Membrane Proteins; Molecular Structure; Plants, Medicinal; Poncirus; Staphylococcal Infections; Staphylococcus aureus | 2020 |
Design, synthesis and biological evaluation of new coumarin-dithiocarbamate hybrids as multifunctional agents for the treatment of Alzheimer's disease.
Topics: Acetylcholinesterase; Alzheimer Disease; Amyloid beta-Peptides; Animals; Blood-Brain Barrier; Cell Line, Tumor; Cholinesterase Inhibitors; Coumarins; Dose-Response Relationship, Drug; Drug Design; Humans; Kinetics; Male; Mice; Mice, Inbred Strains; Models, Molecular; Molecular Structure; Peptide Fragments; Protein Aggregates; Range of Motion, Articular; Structure-Activity Relationship; Thiocarbamates | 2018 |
Assessment of the skin sensitizing potential of chemicals, contained in foods and/or cosmetic ingredients, using a modified local lymph node assay with an elicitation phase (LLNA:DAE) method.
We evaluated the skin sensitizing potential of 10 natural organic chemicals, or their derivatives, which are included in foods and/or skin products, using a modified local lymph node assay (LLNA), with an elicitation phase (LLNA:DAE). The following compounds were tested: carminic acid, esculetin, 4-methyl esculetin, coumarin, quercetin, curcumin, naringenin, chlorogenic acid, isoscopoletin, and shikonin. Esculetin, 4-methyl esculetin, isoscopoletin, and shikonin yielded positive results. In particular, shikonin at a very low concentration (0.05%) induced an elicitation response. In conclusion, four of the 10 natural organic chemicals tested had a skin sensitization potential, with shikonin producing serious reaction even at a very low concentration. Topics: Animals; Carmine; Cosmetics; Coumarins; Curcumin; Dose-Response Relationship, Drug; Female; Food Analysis; Local Lymph Node Assay; Mice, Inbred CBA; Naphthoquinones; Quercetin; Skin; Skin Irritancy Tests; Umbelliferones | 2018 |
Design, synthesis and evaluation of coumarin-pargyline hybrids as novel dual inhibitors of monoamine oxidases and amyloid-β aggregation for the treatment of Alzheimer's disease.
A series of coumarin-pargyline hybrids (4a-x) have been designed, synthesized and evaluated as novel dual inhibitors of Alzheimer's disease (AD). Most of the compounds exhibited a potent ability to inhibit amyloid-β (Aβ) aggregation and monoamine oxidases. In particular, compound 4x exhibited remarkable inhibitory activities against monoamine oxidases (IC Topics: Alzheimer Disease; Amyloid beta-Peptides; Animals; Cell Survival; Coumarins; Dose-Response Relationship, Drug; Drug Design; Humans; Male; Mice; Mice, Inbred Strains; Molecular Structure; Monoamine Oxidase; Monoamine Oxidase Inhibitors; Pargyline; PC12 Cells; Protein Aggregates; Rats; Structure-Activity Relationship | 2017 |