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• W2022604703 abstract "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." @default.
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• W2022604703 date "2012-01-05" @default.
• W2022604703 modified "2023-10-16" @default.
• W2022604703 title "Discovery and Synthesis of Namalide Reveals a New Anabaenopeptin Scaffold and Peptidase Inhibitor" @default.
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• W2022604703 doi "https://doi.org/10.1021/jm201238p" @default.
• W2022604703 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3266974" @default.
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