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Thomas, Douglas D.

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR 2016: 3.273

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1437-4315
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Volume 389, Issue 10 (Oct 2008)

Issues

Cytotoxic and peptidase inhibitory activities of selected non-hepatotoxic cyclic peptides from cyanobacteria

Anja Bubik
  • 1Department of Genetic Toxicology and Cancer Biology, National Institute of Biology, Večna pot 111, POB 141, SI-1001 Ljubljana, Slovenia
/ Bojan Sedmak
  • 2Department of Genetic Toxicology and Cancer Biology, National Institute of Biology, Večna pot 111, POB 141, SI-1001 Ljubljana, Slovenia
/ Marko Novinec
  • 3Department of Biochemistry, Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia
/ Brigita Lenarčič
  • 4Department of Biochemistry, Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia and Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Jamova 39, SI-1000 Ljubljana, Slovenia
/ Tamara T. Lah
  • 5Department of Genetic Toxicology and Cancer Biology, National Institute of Biology, Večna pot 111, POB 141, SI-1001 Ljubljana, Slovenia and Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Jamova 39, SI-1000 Ljubljana, Slovenia
Published Online: 2008-08-19 | DOI: https://doi.org/10.1515/BC.2008.153

Abstract

Toxic cyanobacterial blooms are a rich source of metabolites having a variety of biological activities. Two main groups of cyclic peptides, depsipeptides and ureido linkage-containing peptides, reportedly inhibit serine peptidases. We characterised their inhibitory properties against selected peptidases and investigated their influence on cell viability. The depsipeptide planktopeptin BL1125 is a strong linear competitive tight-binding inhibitor of leukocyte (K i=2.9 nm) and pancreatic (K i=7.2 nm) elastase and also of chymotrypsin (K i=6.1 nm). Anabaenopeptins B and F show no inhibition against chymotrypsin, but inhibit both elastases. The tested cyclic peptides do not inhibit trypsin, urokinase, kallikrein 1 or cysteine peptidases. All three tested cyanopeptides show no short-term cytotoxicity in concentrations of up to 10 μm, but impair the metabolic activity of normal human astrocytes after prolonged exposure (48–96 h), whereas glioblastoma cells, tumour cells of the same type, are resistant. Strong inhibition and relative selectivity of the tested cyanopeptides suggests that they are potential candidates for application in inflammatory diseases and possibly some types of cancers.

Keywords: anabaenopeptin; cyanopeptides; cytotoxicity; planktopeptin; Planktothrix rubescens; protease inhibition

About the article

Corresponding author


Received: 2008-05-13

Accepted: 2008-07-04

Published Online: 2008-08-19

Published in Print: 2008-10-01



Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.153. Export Citation

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