1235885-06-9Relevant academic research and scientific papers
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.
, p. 735 - 742 (2012)
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.
