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Multiple Toxin Production in the Cyanobacterium Microcystis : Isolation of the Toxic Protease Inhibitor Cyanopeptolin 1020
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 462465
Author(s) Gademann, K.; Portmann, C.; Blom, J. F.; Zeder, M.; Juttner, F.
Author(s) at UniBasel Gademann, Karl
Year 2010
Title Multiple Toxin Production in the Cyanobacterium Microcystis : Isolation of the Toxic Protease Inhibitor Cyanopeptolin 1020
Journal Journal of Natural Products
Volume 73
Number 5
Pages / Article-Number 980-4
Abstract The isolation and structure of cyanopeptolin 1020 (hexanoic acid-Glu-N[-O-Thr-Arg-Ahp-Phe-N-Me-Tyr-Val-]) from a Microcystis strain is reported. Very potent picomolar trypsin inhibition (IC50 = 670 pM) and low nanomolar values against human kallikrein (4.5 nM) and factor XIa (3.9 nM) have been determined for cyanopeptolin 1020. For plasmin and chymotrypsin, low micromolar concentrations were necessary for 50% inhibition. Cyanopeptolin 1020 was found to be toxic against the freshwater crustaceanThamnocephalus platyurus (LC50 = 8.8 μM), which is in the same range as some of the well-known microcystins. These data support the hypothesis that cyanopeptolins can be considered as a second class of toxins in addition to the well-established microcystins inMicrocystis.
Publisher American Chemical Society
ISSN/ISBN 0163-3864 ; 1520-6025
edoc-URL http://edoc.unibas.ch/dok/A5841599
Full Text on edoc Restricted
Digital Object Identifier DOI 10.1021/np900818c
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/20405925
ISI-Number WOS:000278080900035
Document type (ISI) Journal Article
 
   

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