Chelidonium majus; Zanthorμlum nitidum(Roxb.)DC.
[1,3]Benzodioxolo[5,6-c]phenanthridinium, 1,2-dimethoxy-12-methyl-, chloride (1:1)/1,2-Dimethoxy-12-methyl[1,3]dioxolo[4,5]benzo[1,2-c]phenanthridin-12-iumchlorid/1,2-dimethoxy-12-methyl[1,3]benzodioxolo[5,6-c]phenanthridiniumchloride/1,2-Dimethoxy-12-methyl[1,3]benzodioxolo[5,6-c]phenanthridin-12-ium chloride/1,2-Dimethoxy-N-methyl(1,3)benzodioxolo(5,6-c)phenanthridinium chloride/1,2-dimethoxy-12-methyl-[1,3]benzodioxolo[5,6-c]phenanthridin-12-ium,chloride/Chelerythrine chloride
Chelerythrine Chloride is a potent, cell-permeable inhibitor of protein kinase C, with an IC50 of 660 nM.
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provides coniferyl ferulate(CAS#:3895-92-9) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Chelerythrine (CHE), a benzophenanthridine alkaloid, is usually used as a nutritional and functional additive in variety of health foods. However, it should be paid enough attention because of its potential toxicity to human health. In this work, the binding mechanism of CHE with bovine serum albumin (BSA) was systematically investigated with spectroscopic approaches. The results showed that the mixture of BSA with CHE could spontaneously cause the formation of BSA-CHE complex through electrostatic interaction under simulative physiological conditions (0.01?mol?L-1 Tris-HCl, 0.015?mol?L-1 NaCl, pH?=?7.4). Site marker competitive displacement experiments exhibited that CHE was primarily bound to the hydrophobic pocket of the site II (subdomain IIIA) of BSA. It has been reported that the binding of small functional molecules to serum albumins remarkably impacts their absorption, distribution, metabolism, conformation, and excretion features. Therefore, this study might be helpful for human to have an in-depth understanding of the biological effect of CHE in vivo and guide human to take it safely and reasonably.
Copyright ? 2019 Elsevier Ltd. All rights reserved.
Binding mechanism; Bovine serum albumin; Chelerythrine; Spectroscopic approaches; Toxicity
Evaluation the binding of chelerythrine, a potentially harmful toxin, with bovine serum albumin.
Shen Y1, Zhu C1, Wang Y1, Xu J1, Xue R1, Ji F1, Wu Y2, Wu Z1, Zhang W1, Zheng Z3, Ye Y4.
Isoquinoline alkaloids possess broad pharmacological activities. In this study, the antifungal activity of twelve isoquinoline alkaloids, including berberine (1), jatrorrhizine (2), coptisine (3), corydaline (4), tetrahydroberberine (5), chelidonine (6), dihydrosanguinarine (7), chelerythrine (8), sanguinarine (9), palmatine (10), tetrahydropalmatine (11) and columbamine (12) were evaluated against eight plant pathogenic fungi in vitro. All the tested compounds showed varying degrees of inhibition against the eight tested plant fungi. Among them, sanguinarine exhibited high antifungal activity (EC50 ranging from 6.96-59.36?μg/mL). It displayed the best inhibitory activity against Magnaporthe oryzae (EC50?=?6.96?μg/mL), compared with azoxystrobin (EC50?=?12.04?μg/mL), and significantly suppressed spore germination of M. oryzae with the inhibition rate reaching 100% (50?μg/mL). The optical microscopy and scanning electron microscopy observations revealed that after treating M. oryzae mycelia with sanguinarine at 10?μg/mL, the mycelia appeared curved, collapsed and the cell membrane integrity was eventually damaged. Furthermore, the reactive oxygen species production, mitochondrial membrane potential and nuclear morphometry of mycelia had been changed, and the membrane function and cell proliferation of mycelia were destroyed. These results will enrich our insights into action mechanisms of antifungal activity of sanguinarine against M. oryzae.
Copyright ? 2019 Elsevier Inc. All rights reserved.
Fungicidal activity; Isoquinoline alkaloids; Sanguinarine
Anti-phytopathogenic activity and the possible mechanisms of action of isoquinoline alkaloid sanguinarine.
Zhao ZM1, Shang XF2, Lawoe RK1, Liu YQ3, Zhou R1, Sun Y1, Yan YF1, Li JC1, Yang GZ1, Yang CJ1.
Chelerythrine (CHL) is a pharmacologically important molecule that appears in positively charged iminium and neutral alkanolamine form on varying the pH. Association of bovine hemoglobin (BHb) with iminium and alkanolamine forms of CHL is explored employing several spectroscopic and theoretical tools. Our results revealed that iminium form of CHL shows greater binding affinity than the neutral alkanolamine form, with nearly one binding site on the protein for both forms. Thermodynamic data showed that the iminium binding to BHb was characterized by negative enthalpy and positive entropy changes while the association of the alkanolamine CHL was accompanied with both positive enthalpy and entropy changes. Both forms of CHL have been found to quench the intrinsic fluorescence of BHb. From Forster’s resonance energy transfer (FRET) studies, the binding distance between the energy acceptor (CHL) and donor (β-Trp 37 of BHb) was found to be optimum for fluorescence quenching to occur. The conformational transformation of BHb induced by CHL complexation showed greater unfolding of the protein architecture for the iminium interaction from CD spectroscopy. Molecular docking study revealed that both iminium and alkanolamine form of CHL reside near β-Trp 37 at the α1β2 interface of BHb.
Copyright ? 2019 Elsevier B.V. All rights reserved.
Acid-alkaline transition; Molecular docking simulation; Protein-drug interaction; Thermodynamics
Elucidation of the association of potential chemotherapeutic alkaloid chelerythrine with bovine hemoglobin by experimental probing and molecular docking simulation.
Bhuiya S1, Chowdhury S1, Haque L1, Das S2.
2019 Oct 1