Journal
MARINE DRUGS
Volume 15, Issue 6, Pages -Publisher
MDPI AG
DOI: 10.3390/md15060191
Keywords
PTP1B; cladosporin; asperentin; Aspergillus; deep-sea
Categories
Funding
- DFG [GU1233/1-1]
- DFG (Center for Integrated Protein Science Munich, CIPSM)
- German Research Foundation (DFG)
- Technical University of Munich (TUM)
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In the frame of studies on secondary metabolites produced by fungi from deep-sea environments we have investigated inhibitors of enzymes playing key roles in signaling cascades of biochemical pathways relevant for the treatment of diseases. Here we report on a new inhibitor of the human protein tyrosine phosphatase 1B (PTP1B), a target in the signaling pathway of insulin. A new asperentin analog is produced by an Aspergillussydowii strain isolated from the sediment of the deep Mediterranean Sea. Asperentin B (1) contains an additional phenolic hydroxy function at C-6 and exhibits an IC50 value against PTP1B of 2 M in vitro, which is six times stronger than the positive control, suramin. Interestingly, asperentin (2) did not show any inhibition of this enzymatic activity. Asperentin B (1) is discussed as possible therapeutic agents for type 2 diabetes and sleeping sickness.
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