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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
Published on: January 26, 2016
Tiglicamides A-C, cyclodepsipeptides from the marine cyanobacterium Lyngbya confervoides
Susan Matthew1, Valerie J Paul, Hendrik Luesch
1Department of Medicinal Chemistry, University of Florida, Gainesville, Florida 32610, USA.
Abstract:
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 IC(50) values from 2.14 to 7.28 microM. 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.
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