178357-84-1Relevant articles and documents
Bisebromoamide, a potent cytotoxic peptide from the marine cyanobacterium lyngbya sp.: Isolation, stereostructure, and biological activity
Teruya, Toshiaki,Sasaki, Hiroaki,Fukazawa, Hidesuke,Suenaga, Kiyotake
, p. 5062 - 5065 (2009)
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
Revised structure and structure-activity relationship of bisebromoamide and structure of norbisebromoamide from the marine cyanobacterium Lyngbya sp.
Sasaki, Hiroaki,Teruya, Toshiaki,Fukazawa, Hidesuke,Suenaga, Kiyotake
experimental part, p. 990 - 994 (2011/03/19)
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.
