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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1989 Feb;86(3):770–774. doi: 10.1073/pnas.86.3.770

Structural characterization of toxic cyclic peptides from blue-green algae by tandem mass spectrometry.

T Krishnamurthy 1, L Szafraniec 1, D F Hunt 1, J Shabanowitz 1, J R Yates 3rd 1, C R Hauer 1, W W Carmichael 1, O Skulberg 1, G A Codd 1, S Missler 1
PMCID: PMC286558  PMID: 2492662

Abstract

Combined use of chemical degradation, derivatization, and tandem mass spectrometry for rapid structural characterization of toxic cyclic peptides from blue-green algae at the nanomole level is described. Previously, all blue-green algal toxins were thought to belong to a family of seven-residue cyclic peptides, having the general structure cyclo-D-Ala-L-Xaa-erythro-beta-methyl-D-isoaspartic acid-L-Yaa-Adda-D-isoglutamic acid-N-methyldehydroalanine, where Xaa and Yaa represent variable amino acids of the L configuration and Adda is 3-amino-9-methoxy-2,6,8-trimethyl-10-phenyl-deca-4,6-dienoic acid. Structural characterization of two additional toxins indicates that further variability can exist within this family of naturally occurring toxic cyclic peptides. Isoaspartic acid and dehydroalanine can substitute for beta-methylisoaspartic acid and N-methyldehydroalanine, respectively.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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