Calmodulin inhibitors from aspergillus stromatoides. González-Andrade, M., Del Valle, P., Macías-Rubalcava, M., Sosa-Peinado, A., Del Carmen González, M., & Mata, R. Chemistry and Biodiversity, 2013. abstract bibtex An organic extract was prepared from the culture medium and mycelia of the marine fungus Aspergillus stromatoides Raper & Fennell. The extract was fractionated via column chromatography, and the resulting fractions were tested for their abilities to quench the fluorescence of the calmodulin (CaM) biosensor hCaM M124C-mBBr. From the active fraction, emodin (1) and ω-hydroxyemodin (2) were isolated as CaM inhibitors. Anthraquinones 1 and 2 quenched the fluorescence of the hCaM M124C-mBBr biosensor in a concentration-dependent manner with K d values of 0.33 and 0.76 μM, respectively. The results were compared with those of chlorpromazine (CPZ), a classical inhibitor of CaM, with a K d value of 1.25 μM. Docking analysis revealed that 1 and 2 bind to the same pocket of CPZ. The CaM inhibitor properties of 1 and 2 were correlated with some of their reported biological properties. Citrinin (3), methyl 8-hydroxy-6-methyl-9-oxo-9H-xanthene-1-carboxylate (4), and coniochaetone A (5) were also isolated in the present study. The X-ray structure of 5 is reported for the first time. Copyright © 2013 Verlag Helvetica Chimica Acta AG, Zürich.
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title = {Calmodulin inhibitors from aspergillus stromatoides},
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abstract = {An organic extract was prepared from the culture medium and mycelia of the marine fungus Aspergillus stromatoides Raper & Fennell. The extract was fractionated via column chromatography, and the resulting fractions were tested for their abilities to quench the fluorescence of the calmodulin (CaM) biosensor hCaM M124C-mBBr. From the active fraction, emodin (1) and ω-hydroxyemodin (2) were isolated as CaM inhibitors. Anthraquinones 1 and 2 quenched the fluorescence of the hCaM M124C-mBBr biosensor in a concentration-dependent manner with K d values of 0.33 and 0.76 μM, respectively. The results were compared with those of chlorpromazine (CPZ), a classical inhibitor of CaM, with a K d value of 1.25 μM. Docking analysis revealed that 1 and 2 bind to the same pocket of CPZ. The CaM inhibitor properties of 1 and 2 were correlated with some of their reported biological properties. Citrinin (3), methyl 8-hydroxy-6-methyl-9-oxo-9H-xanthene-1-carboxylate (4), and coniochaetone A (5) were also isolated in the present study. The X-ray structure of 5 is reported for the first time. Copyright © 2013 Verlag Helvetica Chimica Acta AG, Zürich.},
bibtype = {article},
author = {González-Andrade, M. and Del Valle, P. and Macías-Rubalcava, M.L. and Sosa-Peinado, A. and Del Carmen González, M. and Mata, R.},
journal = {Chemistry and Biodiversity},
number = {3}
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