Journal
PHYTOCHEMISTRY
Volume 70, Issue 17-18, Pages 2058-2063Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.phytochem.2009.09.010
Keywords
Marine cyanobacteria; Lyngbya confervoides; Cyclodepsipeptides; Nonribosomal peptide synthesis; Elastase inhibitors
Categories
Funding
- NIGMS NIH HHS [P41 GM086210-01S1, P41 GM086210-01, P41 GM086210, P41GM086210] Funding Source: Medline
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The Floridian marine cyanobacterium Lyngbya confervoides afforded cyclodepsipeptides, termed tiglicamides A-C (1-3), along with their previously reported analogues largamides A-C (4-6), all of which possess an unusual tiglic acid moiety. Their structures were deduced by one- and two-dimensional NMR combined with mass spectrometry and the absolute configurations established by chiral HPLC and Marfey's analysis of the degradation products. Compounds 1-3 moderately inhibited porcine pancreatic elastase in vitro with IC50 values from 2.14 to 7.28 mu M. Compounds 1-6 differ from each other by one amino acid residue within the cyclic core structure, suggesting an unusually relaxed substrate specificity of the nonribosomal peptide synthetase that is the putative biosynthetic enzyme responsible for the corresponding amino acid incorporation. (C) 2009 Elsevier Ltd. All rights reserved.
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