Nyuzenamide C, an Antiangiogenic Epoxy Cinnamic Acid-Containing Bicyclic Peptide from a Riverine Streptomyces sp.

Joon Soo An, Myoun Su Kim, Jaeho Han, Sung Chul Jang, Ji Hyeon Im, Jinsheng Cui, Yeonjin Lee, Sang Jip Nam, Jongheon Shin, Sang Kook Lee, Yeo Joon Yoon, Dong Chan Oh

Research output: Contribution to journalReview articlepeer-review

13 Scopus citations

Abstract

A new nonribosomal peptide, nyuzenamide C (1), was discovered from riverine sediment-derived Streptomyces sp. DM14. Comprehensive analysis of the spectroscopic data of nyuzenamide C (1) revealed that 1 has a bicyclic backbone composed of six common amino acid residues (Asn, Leu, Pro, Gly, Val, and Thr) and four nonproteinogenic amino acid units, including hydroxyglycine, β-hydroxyphenylalanine, p-hydroxyphenylglycine, and 3,β-dihydroxytyrosine, along with 1,2-epoxypropyl cinnamic acid. The absolute configuration of 1 was proposed by J-based configuration analysis, the advanced Marfey's method, quantum mechanics-based DP4 calculations, and bioinformatic analysis of its nonribosomal peptide synthetase biosynthetic gene cluster. Nyuzenamide C (1) displayed antiangiogenic activity in human umbilical vein endothelial cells and induced quinone reductase in murine Hepa-1c1c7 cells.

Original languageEnglish
Pages (from-to)804-814
Number of pages11
JournalJournal of Natural Products
Volume85
Issue number4
DOIs
StatePublished - 22 Apr 2022

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