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Mar. Drugs 2017, 15(6), 191;

Asperentin B, a New Inhibitor of the Protein Tyrosine Phosphatase 1B

GEOMAR Helmholtz Center for Ocean Research Kiel, RD3 Marine Microbiology, Düsternbrooker Weg 20, 24105 Kiel, Germany
Department of Chemistry and Center for Integrated Protein Science Munich (CIPSM), Biosystems Chemistry, Technical University of Munich, Lichtenbergstraße 4, 85747 Garching, Germany
Authors to whom correspondence should be addressed.
Academic Editor: Russell Kerr
Received: 31 January 2017 / Revised: 13 June 2017 / Accepted: 17 June 2017 / Published: 21 June 2017
(This article belongs to the Special Issue Marine Fungal Natural Products)
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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 Aspergillus sydowii 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 μM 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. View Full-Text
Keywords: PTP1B; cladosporin; asperentin; Aspergillus; deep-sea PTP1B; cladosporin; asperentin; Aspergillus; deep-sea

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Wiese, J.; Aldemir, H.; Schmaljohann, R.; Gulder, T.A.M.; Imhoff, J.F. Asperentin B, a New Inhibitor of the Protein Tyrosine Phosphatase 1B. Mar. Drugs 2017, 15, 191.

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