@article{PimentelElardoBubackGulderetal.2011,
  author    = {Pimentel-Elardo, Sheila M. and Buback, Verena and Gulder, Tobias A. M. and Bugni, Tim S. and Reppart, Jason and Bringmann, Gerhard and Ireland, Chris M. and Schirmeister, Tanja and Hentschel, Ute},
  title     = {New Tetromycin Derivatives with Anti-Trypanosomal and Protease Inhibitory Activities},
  series = {Marine drugs},
  volume    = {9},
  journal   = {Marine drugs},
  number    = {10},
  doi       = {10.3390/md9101682},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-141171},
  pages     = {1682-1697},
  year      = {2011},
  abstract  = {Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001(T) cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV M(pro), and PL(pro). The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteases with K(i) values in the low micromolar range.},
  language  = {en}
}
@article{PimentelElardoBubackGulderetal.2011,
  author    = {Pimentel-Elardo, Sheila M. and Buback, Verena and Gulder, Tobias A. M. and Bugni, Tim S. and Reppart, Jason and Bringmann, Gerhard and Ireland, Chris M. and Schirmeister, Tanja and Hentschel, Ute},
  title     = {New Tetromycin Derivatives with Anti-Trypanosomal and Protease Inhibitory Activities},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-75465},
  year      = {2011},
  abstract  = {Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001T cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV Mpro, and PLpro. The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteases with Ki values in the low micromolar range.},
  subject      = {Biologie},
  language  = {en}
}
@article{OliAbdelmohsenHentscheletal.2014,
  author    = {Oli, Swarna and Abdelmohsen, Usama Ramadan and Hentschel, Ute and Schirmeister, Tanja},
  title     = {Identification of Plakortide E from the Caribbean Sponge Plakortis halichondroides as a Trypanocidal Protease Inhibitor using Bioactivity-Guided Fractionation},
  series = {MARINE DRUGS},
  volume    = {12},
  journal   = {MARINE DRUGS},
  number    = {5},
  issn      = {1660-3397},
  doi       = {10.3390/md12052614},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-116536},
  pages     = {2614-2622},
  year      = {2014},
  abstract  = {In this paper, we report new protease inhibitory activity of plakortide E towards cathepsins and cathepsin-like parasitic proteases. We further report on its anti-parasitic activity against Trypanosoma brucei with an IC50 value of 5 mu M and without cytotoxic effects against J774.1 macrophages at 100 mu M concentration. Plakortide E was isolated from the sponge Plakortis halichondroides using enzyme assay-guided fractionation and identified by NMR spectroscopy and mass spectrometry. Furthermore, enzyme kinetic studies confirmed plakortide E as a non-competitive, slowly-binding, reversible inhibitor of rhodesain.},
  language  = {en}
}
@article{AbdelmohsenSzesnyOthmanetal.2012,
  author    = {Abdelmohsen, Usama Ramadan and Szesny, Matthias and Othman, Eman Maher and Schirmeister, Tanja and Grond, Stepanie and Stopper, Helga and Hentschel, Ute},
  title     = {Antioxidant and Anti-Protease Activities of Diazepinomicin from the Sponge-Associated Micromonospora Strain RV115},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-76279},
  year      = {2012},
  abstract  = {Diazepinomicin is a dibenzodiazepine alkaloid with an unusual structure among the known microbial metabolites discovered so far. Diazepinomicin was isolated from the marine sponge-associated strain Micromonospora sp. RV115 and was identified by spectroscopic analysis and by comparison to literature data. In addition to its interesting preclinical broad-spectrum antitumor potential, we report here new antioxidant and anti-protease activities for this compound. Using the ferric reducing antioxidant power (FRAP) assay, a strong antioxidant potential of diazepinomicin was demonstrated. Moreover, diazepinomicin showed a significant antioxidant and protective capacity from genomic damage induced by the reactive oxygen species hydrogen peroxide in human kidney (HK-2) and human promyelocytic (HL-60) cell lines. Additionally, diazepinomicin inhibited the proteases rhodesain and cathepsin L at an IC50 of 70-90 μM. It also showed antiparasitic activity against trypomastigote forms of Trypanosoma brucei with an IC50 of 13.5 μM. These results showed unprecedented antioxidant and anti-protease activities of diazepinomicin, thus further highlighting its potential as a future drug candidate.},
  subject      = {Biologie},
  language  = {en}
}