Structures and Activity of New Anabaenopeptins Produced by Baltic Sea Cyanobacteria

Anabaenopeptins, bioactive cyclic hexapeptides, were isolated by preparative reversed-phase high performance liquid chromatography from an extract of Baltic Sea cyanobacterial bloom material composed of Nodularia spumigena (50%), Aphanizomenon flos-aquae (40%) and Dolichospermum spp. (10%). Five new...

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Bibliographic Details
Published in:Marine drugs 2015-12, Vol.14 (1), p.8-8
Main Authors: Spoof, Lisa, Błaszczyk, Agata, Meriluoto, Jussi, Cegłowska, Marta, Mazur-Marzec, Hanna
Format: Article
Language:English
Subjects:
Anabaenopeptins
Aphanizomenon flos-aquae
Baltic Sea
Baltic States
carboxypeptidase A
Chromatography, High Pressure Liquid
cyanobacteria
Cyanobacteria - chemistry
Dolichospermum spp
Enzyme Inhibitors - chemistry
Humans
Marine
nodulapeptins
Nodularia spumigena
Pancreatic Elastase - antagonists & inhibitors
Peptides, Cyclic - chemistry
Phosphoric Monoester Hydrolases - antagonists & inhibitors
protein phosphatase 1
Seawater
Structure-Activity Relationship
Tandem Mass Spectrometry
Thrombin - antagonists & inhibitors
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Summary:Anabaenopeptins, bioactive cyclic hexapeptides, were isolated by preparative reversed-phase high performance liquid chromatography from an extract of Baltic Sea cyanobacterial bloom material composed of Nodularia spumigena (50%), Aphanizomenon flos-aquae (40%) and Dolichospermum spp. (10%). Five new anabaenopeptins and nine previously known anabaenopeptins were isolated, and their putative structures were determined by tandem mass spectrometry. The activity of the peptides against carboxypeptidase A and protein phosphatase 1 as well as chymotrypsin, trypsin and thrombin was tested. All anabaenopeptins inhibited carboxypeptidase A (apart from one anabaenopeptin variant) and protein phosphatase 1 with varying potency, but no inhibition against chymotrypsin, trypsin and thrombin was observed.
ISSN:1660-3397
1660-3397
DOI:10.3390/md14010008