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

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

  • J Nat Prod. 2022 Apr 22;85(4):804-814. doi: 10.1021/acs.jnatprod.1c00837.
Joon Soo An 1,  Myoun-Su Kim 1,  Jaeho Han 1,  Sung Chul Jang 1,  Ji Hyeon Im 1,  Jinsheng Cui 1,  Yeonjin Lee 1,  Sang-Jip Nam 2,  Jongheon Shin 1,  Sang Kook Lee 1,  Yeo Joon Yoon 1,  Dong-Chan Oh 1
Affiliations

Affiliations

  • 1 Natural Products Research Institute, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea.
  • 2 Department of Chemistry and Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea.
PMID: 35294831 DOI: 10.1021/acs.jnatprod.1c00837
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.

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