60280-45-7Relevant articles and documents
Metabolomics-Guided Discovery of Microginin Peptides from Cultures of the Cyanobacterium Microcystis aeruginosa
Stewart, Allison K.,Ravindra, Rudravajhala,Van Wagoner, Ryan M.,Wright, Jeffrey L. C.
, p. 349 - 355 (2018)
We report a mass-spectrometry-based metabolomics study of a laboratory-cultured strain of Microcystis aeruginosa (UTEX LB2385), which has led to the discovery of five peptides (1-5) belonging to the microginin class of linear cyanopeptides. The structures and configurations of these peptides were determined by spectroscopic analyses and chemical derivitization. The microginin peptides described herein are the first reported derivatives containing N-methyl methionine (1, 5) and N-methyl methionine sulfoxide (2-4). The two tripeptide microginin analogues (4, 5) identified represent the smallest members of this peptide family. Their angiotensin-converting enzyme (ACE) inhibitory activity was also investigated. Microginin 527 (4) was the most potent of the group, with an IC50 of 31 μM.
Resolution of the Confusion in the Assignments of Configuration for the Ciliatamides, Acylated Dipeptides from Marine Sponges
Takada, Kentaro,Irie, Raku,Suo, Rei,Matsunaga, Shigeki
, p. 2845 - 2849 (2017/11/06)
Direct comparison of authentic ciliatamide A with four synthetic isomers (1-4) by means of NMR and chiral-phase HPLC revealed that ciliatamide A possesses the 12R (d-N-MePhe residue) and 22S (l-Lys residue) configurations, which were not identical with either our previous assignment or those proposed by others through total synthesis. The absolute configuration of the methionine sulfoxide residue in ciliatamide D was also revised to be d.
The synthesis of precursors of labelled neuropeptides
Van Nispen,Bijl,Hendrix,Greven
, p. 276 - 283 (2007/10/02)
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