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  • 1
    In: Plants, MDPI AG, Vol. 11, No. 3 ( 2022-01-30), p. 388-
    Kurzfassung: The phytochemical constituents from the roots of Millettia speciosa were investigated by chromatographic isolation, and their chemical structures were characterized using the MS and NMR spectroscopic methods. A total of 10 compounds, including six triterpenoids, two flavonoids, and two phenolic compounds, were identified from the roots of M. speciosa. Out of the isolated compounds, eight showed inhibitory effects on NO production in lipopolysaccharide (LPS)-stimulated RAW 264.7 cells, with IC50 values ranging from 43.9 to 449.5 µg/mL. Ursane-type triterpenes significantly suppressed NO production compared to the remaining compounds. In addition, these compounds also exhibited remarkable inhibitory effects on α-glucosidase. Among the tested compounds, 4, 5, and 10 exhibited excellent α-glucosidase inhibition, with IC50 values ranging from 1.1 to 2.2 µg/mL. Almost all of the test compounds showed little or no acetylcholinesterase inhibition, except for 5, which showed moderate anti-acetylcholinesterase activity in vitro. The molecular docking study of α-glucosidase inhibition by 3–5 and 10 was conducted to observe the interactions of these molecules with the enzyme. Compounds 4, 5, and 10 exhibited a better binding affinity toward the targeted receptor and the H-bond interactions located at the entrance of the enzyme active site pocket in comparison to those of 3 and the positive control acarbose. Our findings evidence the pharmacological potential of this species and suggest that the phytochemicals derived from the roots of M. speciosa may be promising lead molecules for further studies on the development of anti-inflammatory and anti-diabetes drugs.
    Materialart: Online-Ressource
    ISSN: 2223-7747
    Sprache: Englisch
    Verlag: MDPI AG
    Publikationsdatum: 2022
    ZDB Id: 2704341-1
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 2
    In: Applied Sciences, MDPI AG, Vol. 9, No. 7 ( 2019-04-08), p. 1473-
    Kurzfassung: In this work, we investigate a novel approach to prepare high-performance alpha-particle solid sources fabricated on diamond thin support layers, offering the properties of diamond such as a low-Z material with corrosion and mechanical hardness. As-prepared solid sources onto boron-doped-diamond (BDD) substrate exhibited high performance of the autoradiography and spectroscopic resolution at the level of other more conventional materials such as stainless steel. A straightforward precipitation process in the Na2SO4 or NaNO3 simple electrolytes under mild experimental conditions with a low current of several mA.cm−2 were successfully developed onto BDD substrates for deposition of single 241Am as well as 239Pu, 241Am, and 244Cm mixed radionuclides. The results demonstrate that solid sources deposited onto such BDD substrates can match the performance of those prepared onto stainless steel substrates with excellent uniformity and high-resolution spectroscopy, together combining the robustness, chemical resilience, and X-ray transparence of the diamond. Alpha-particle spectra exhibiting a low full width at half maximum (FWHM) of 12.5 keV at the energy of 5.485 MeV (241Am) could be practically obtained for BDD substrates.
    Materialart: Online-Ressource
    ISSN: 2076-3417
    Sprache: Englisch
    Verlag: MDPI AG
    Publikationsdatum: 2019
    ZDB Id: 2704225-X
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 3
    In: Molecules, MDPI AG, Vol. 27, No. 7 ( 2022-03-28), p. 2204-
    Kurzfassung: Epigenetic alterations found in all human cancers are promising targets for anticancer therapy. In this sense, histone deacetylase inhibitors (HDACIs) are interesting anticancer agents that play an important role in the epigenetic regulation of cancer cells. Here, we report 15 novel hydroxamic acid-based histone deacetylase inhibitors with quinazolinone core structures. Five compounds exhibited antiproliferative activity with IC50 values of 3.4–37.8 µM. Compound 8 with a 2-mercaptoquinazolinone cap moiety displayed the highest antiproliferative efficacy against MCF-7 cells. For the HDAC6 target selectivity study, compound 8 displayed an IC50 value of 2.3 µM, which is 29.3 times higher than those of HDAC3, HDAC4, HDAC8, and HDAC11. Western blot assay proved that compound 8 strongly inhibited tubulin acetylation, a substrate of HDAC6. Compound 8 also displayed stronger inhibition activity against HDAC11 than the control drug Belinostat. The inhibitory mechanism of action of compound 8 on HDAC enzymes was then explored using molecular docking study. The data revealed a high binding affinity (−7.92 kcal/mol) of compound 8 toward HDAC6. In addition, dock pose analysis also proved that compound 8 might serve as a potent inhibitor of HDAC11.
    Materialart: Online-Ressource
    ISSN: 1420-3049
    Sprache: Englisch
    Verlag: MDPI AG
    Publikationsdatum: 2022
    ZDB Id: 2008644-1
    Standort Signatur Einschränkungen Verfügbarkeit
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