850863-77-3Relevant articles and documents
Solid-Phase Total Synthesis of Oscillamide Y and Analogues
Marsh, Ian R.,Bradley, Mark,Teague, Simon J.
, p. 6199 - 6203 (1997)
We report an efficient solid phase synthesis of oscillamide Y and three analogues. The cyclic peptide was prepared using a combination of Fmoc and allyl chemistries and an acid labile Wang type linker. The urea functionality was smoothly incorporated usin
Homophymamide A, Heterodetic Cyclic Tetrapeptide from a Homophymia sp. Marine Sponge: A Cautionary Note on Configurational Assignment of Peptides That Contain a Ureido Linkage
Arakawa, Osamu,Ise, Yuji,Kanki, Daichi,Matsunaga, Shigeki,Morii, Yasuhiro,Nakamukai, Shohei,Ogura, Yusuke,Okada, Shigeru,Takatani, Tomohiro,Takikawa, Hirosato,Yamawaki, Nobuhiro
, p. 1848 - 1853 (2021)
A previously unreported heterodetic cyclic peptide, homophymamide A (1), was isolated from a Homophymia sp. marine sponge. The structure of homophymamide A was determined to be a lower homologue of anabaenopeptins by spectroscopic analysis, chemical degradation, and chemical synthesis. Analysis of the acidic hydrolysate showed that the racemization of Lys took place, leading us to pose a cautionary note on the configurational assignment of peptides that contain a ureido bond.
Discovery and synthesis of namalide reveals a new anabaenopeptin scaffold and peptidase inhibitor
Cheruku, Pradeep,Plaza, Alberto,Lauro, Gianluigi,Keffer, Jessica,Lloyd, John R.,Bifulco, Giuseppe,Bewley, Carole A.
supporting information; experimental part, p. 735 - 742 (2012/03/27)
The discovery, structure elucidation, and solid-phase synthesis of namalide, a marine natural product, are described. Namalide is a cyclic tetrapeptide; its macrocycle is formed by only three amino acids, with an exocyclic ureido phenylalanine moiety at its C-terminus. The absolute configuration of namalide was established, and analogs were generated through Fmoc-based solid phase peptide synthesis. We found that only natural namalide and not its analogs containing l-Lys or l-allo-Ile inhibited carboxypeptidase A at submicromolar concentrations. In parallel, an inverse virtual screening approach aimed at identifying protein targets of namalide selected carboxypeptidase A as the third highest scoring hit. Namalide represents a new anabaenopeptin-type scaffold, and its protease inhibitory activity demonstrates that the 13-membered macrolactam can exhibit similar activity as the more common hexapeptides.
