Bisebromoamide, a potent cytotoxic peptide from the marine cyanobacterium Lyngbya sp.: isolation, stereostructure, and biological activity

Toshiaki Teruya; Hiroaki Sasaki; Hidesuke Fukazawa; Kiyotake Suenaga

doi:10.1021/ol9020546

Bisebromoamide, a potent cytotoxic peptide from the marine cyanobacterium Lyngbya sp.: isolation, stereostructure, and biological activity

Org Lett. 2009 Nov 5;11(21):5062-5. doi: 10.1021/ol9020546.

Authors

Toshiaki Teruya¹, Hiroaki Sasaki, Hidesuke Fukazawa, Kiyotake Suenaga

Affiliation

¹ Department of Chemistry, Faculty of Science and Technology, Keio University, Hiyoshi 3-14-1, Kohoku-ku, Yokohama 223-8522, Japan.

PMID: 19803465
DOI: 10.1021/ol9020546

Abstract

A novel cytotoxic peptide, termed bisebromoamide (1), has been isolated from the marine cyanobacterium Lyngbya sp. Its planar structure was determined by 1D and 2D NMR spectroscopy. The absolute stereostructure of 1 was determined by chemical degradation followed by chiral HPLC analysis. Bisebromoamide (1) exhibited potent protein kinase inhibition: the phosphorylation of ERK in NRK cells by PDGF-stimulation was selectively inhibited by treatment with 10-0.1 microM of 1.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Anticonvulsants / chemistry
Anticonvulsants / isolation & purification*
Anticonvulsants / pharmacology*
Cyanobacteria / chemistry*
Drug Screening Assays, Antitumor
Extracellular Signal-Regulated MAP Kinases / antagonists & inhibitors
HeLa Cells
Humans
Lyngbya Toxins / chemistry
Lyngbya Toxins / isolation & purification*
Lyngbya Toxins / pharmacology*
Molecular Structure
Nuclear Magnetic Resonance, Biomolecular
Oligopeptides / chemistry
Oligopeptides / isolation & purification*
Oligopeptides / pharmacology*
Protein Kinase Inhibitors / chemistry
Protein Kinase Inhibitors / isolation & purification*
Protein Kinase Inhibitors / pharmacology*

Substances

Anticonvulsants
Lyngbya Toxins
Oligopeptides
Protein Kinase Inhibitors
bisebromoamide
Extracellular Signal-Regulated MAP Kinases