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  • 1
    Online Resource
    Online Resource
    Inhibition of monoamine oxidases by benzimidazole chalcone derivatives
    Springer Science and Business Media LLC ; 2023
    In:  Applied Biological Chemistry Vol. 66, No. 1 ( 2023-06-17)
    Details
    In: Applied Biological Chemistry, Springer Science and Business Media LLC, Vol. 66, No. 1 ( 2023-06-17)
    Abstract: Ten benzimidazole chalcone derivatives were synthesized, and their monoamine oxidase (MAO) inhibitory activity was evaluated. Most compounds showed higher inhibitory activity against MAO-B than MAO-A. Compound BCH2 exhibited an IC 50 value of 0.80 μM, thereby showing the most potent inhibition amongst all. In addition, BCH2 showed the highest MAO-B selectivity index (SI) with an SI value of 44.11 compared to MAO-A. Among the substituents, the halogen group showed the best MAO-B inhibition, and the ortho -position of the B ring showed better inhibitory activity than the para -site. In comparison with ortho -substituents, the inhibitory activity increased in the order, -Cl  〉  -Br  〉  -F  〉  -H. BCH2 was found to be a competitive inhibitor of the enzyme with optimum inhibition kinetics, where K i was found to be 0.25 ± 0.014 μM. In the reversibility experiment, BCH2 showed a recovery pattern after MAO-B inhibition, similar to that of lazabemide. Thus, BCH2 is a potent, reversible, and selective MAO-B inhibitor and has been suggested as a candidate for the treatment of neurological disorders.
    Type of Medium: Online Resource
    ISSN: 2468-0842
    URL: Article
    DOI: 10.1186/s13765-023-00795-1
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2023
    detail.hit.zdb_id: 2846955-0
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  • 2
    Online Resource
    Online Resource
    Development of Halogenated Pyrazolines as Selective Monoamine Oxidase-B Inhibitors: Deciphering via Molecular Dynamics Approach
    MDPI AG ; 2021
    In:  Molecules Vol. 26, No. 11 ( 2021-05-28), p. 3264-
    Details
    In: Molecules, MDPI AG, Vol. 26, No. 11 ( 2021-05-28), p. 3264-
    Abstract: Halogens have been reported to play a major role in the inhibition of monoamine oxidase (MAO), relating to diverse cognitive functions of the central nervous system. Pyrazoline/halogenated pyrazolines were investigated for their inhibitory activities against human monoamine oxidase-A and -B. Halogen substitutions on the phenyl ring located at the fifth position of pyrazoline showed potent MAO-B inhibition. Compound 3-(4-ethoxyphenyl)-5-(4-fluorophenyl)-4,5-dihydro-1H-pyrazole (EH7) showed the highest potency against MAO-B with an IC50 value of 0.063 µM. The potencies against MAO-B were increased in the order of –F (in EH7) 〉 –Cl (EH6) 〉 –Br (EH8) 〉 –H (EH1). The residual activities of most compounds for MAO-A were 〉 50% at 10 µM, except for EH7 and EH8 (IC50 = 8.38 and 4.31 µM, respectively). EH7 showed the highest selectivity index (SI) value of 133.0 for MAO-B, followed by EH6 at 〉 55.8. EH7 was a reversible and competitive inhibitor of MAO-B in kinetic and reversibility experiments with a Ki value of 0.034 ± 0.0067 µM. The molecular dynamics study documented that EH7 had a good binding affinity and motional movement within the active site with high stability. It was observed by MM-PBSA that the chirality had little effect on the overall binding of EH7 to MAO-B. Thus, EH7 can be employed for the development of lead molecules for the treatment of various neurodegenerative disorders.
    Type of Medium: Online Resource
    ISSN: 1420-3049
    URL: Article
    DOI: 10.3390/molecules26113264
    Language: English
    Publisher: MDPI AG
    Publication Date: 2021
    detail.hit.zdb_id: 2008644-1
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  • 3
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    Online Resource
    A comprehensive review of the docking studies of chalcone for the development of selective MAO-B inhibitors
    Bentham Science Publishers Ltd. ; 2023
    In:  CNS & Neurological Disorders - Drug Targets Vol. 22 ( 2023-05-15)
    Details
    In: CNS & Neurological Disorders - Drug Targets, Bentham Science Publishers Ltd., Vol. 22 ( 2023-05-15)
    Abstract: Monoamine oxidase B is a crucial therapeutic target for neurodegenerative disorders like Alzheimer's and Parkinson's since they assist in disintegrating neurotransmitters such as dopamine in the brain. Pursuing efficacious monoamine oxidase B inhibitors is a hot topic, as contemporary therapeutic interventions have many shortcomings. Currently available FDA-approved monoamine oxidase inhibitors like safinamide, selegiline and rasagiline also have a variety of side effects like depression and insomnia. In the quest for a potent monoamine oxidase B inhibitor, sizeable, diverse chemical entities have been uncovered, including chalcones. Chalcone is a renowned structural framework that has been intensively explored for its monoamine oxidase B inhibitory activity.The structural resemblance of chalcone (1,3-diphenyl-2-propen-1-one) based compounds and 1,4-diphenyl-2-butene, a recognized MAO-B inhibitor, accounts for their MAO-B inhibitory activity. Therefore, multiple revisions to the chalcone scaffold have been attempted by the researchers to scrutinize the implications of substitutions onthe molecule's potency. In this work, we outline the docking investigation results of various chalcone analogues with monoamine oxidase B available in the literature until now to understand the interaction modes and influence of substituents. Here we focused on the interactions between reported chalcone derivatives and the active site of monoamine oxidase B and the influence of substitutions on those interactions. Detailed images illustrating the interactions and impact of the substituents or structural modifications on these interactions were used to support the docking results.
    Type of Medium: Online Resource
    ISSN: 1871-5273
    URL: Article
    DOI: 10.2174/1871527322666230515155000
    Language: English
    Publisher: Bentham Science Publishers Ltd.
    Publication Date: 2023
    SSG: 15,3
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