Revised structure and structure-activity relationship of bisebromoamide and structure of norbisebromoamide from the marine cyanobacterium Lyngbya sp.

Hiroaki Sasaki, Toshiaki Teruya, Hidesuke Fukazawa, Kiyotake Suenaga

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Novel potent cytotoxic peptides bisebromoamide (1) and norbisebromoamide (2) have been isolated from the marine cyanobacterium Lyngbya sp. The planar structure of these peptides was elucidated through the extensive application of 1D and 2D NMR techniques. The absolute stereostructure of 1 was determined by chemical degradation followed by chiral HPLC analysis. Recently, Tao and co-workers achieved synthesis of bisebromoamide, and the configuration of thiazoline moiety was revised. We re-investigated the stereochemistry of thiazoline moiety of 1. The structure-activity relationships of bisebromoamide (1) were investigated with the use of natural and synthetic analogs. Furthermore, bisebromoamide (1) potently inhibited protein kinase: the phosphorylation of ERK in NRK cells by PDGF-stimulation was selectively inhibited by treatment with 10-0.1 μM of 1.

Original languageEnglish
Pages (from-to)990-994
Number of pages5
JournalTetrahedron
Volume67
Issue number5
DOIs
Publication statusPublished - 2011 Feb 4

Keywords

  • Cyanobacteria
  • Cytotoxicity
  • Kinase inhibitor
  • Natural products
  • Peptide

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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