96576-07-7Relevant articles and documents
Lyngbyaureidamides A and B, two anabaenopeptins from the cultured freshwater cyanobacterium Lyngbya sp. (SAG 36.91)
Zi, Jiachen,Lantvit, Daniel D.,Swanson, Steven M.,Orjala, Jimmy
, p. 173 - 177 (2012)
Two anabaenopeptin-type peptides, lyngbyaureidamides A and B, together with two previously reported peptides lyngbyazothrins C and D, were isolated from the cultured freshwater cyanobacterium Lyngbya sp. (SAG 36.91). Their structures were determined by spectroscopic and chemical methods. Lyngbyazothrins C and D were also able to inhibit the 20S proteasome with IC50 values of 7.1 μM and 19.2 μM, respectively, while lyngbyaureidamides A and B were not active at 50 μM.
Homotyrosine-containing cyanopeptolins 880 and 960 and anabaenopeptins 908 and 915 from Planktothrix agardhii CYA 126/8
Okumura, Hilary S.,Philmus, Benjamin,Portmann, Cyril,Hemscheidt, Thomas K.
supporting information; experimental part, p. 172 - 176 (2009/06/27)
Two homotyrosine-bearing cyanopeptolins are described from Planktothrix agardhii CYA 126/8. The compounds feature a common homotyrosine-containing cyclohexadepsipeptide and differ by sulfation of an exocyclically located 2-O-methyl-D-glyceric acid residue. In addition we describe two anabaenopeptins, which contain two homotyrosine residues, one of which is N-methylated. The anabaenopeptins have a common cyclopentapeptide portion and differ in the amino acid linked to it via an ureido bond, arginine and tyrosine, respectively.
HYDROXYLATION REACTION OF AROMATIC RINGS IN AQUEOUS SOLUTION INDUCED BY HYDROGEN-OXYGEN FLAME
Takasaki, Michiaki,Nomoto, Shinya,Harada, Kaoru
, p. 1629 - 1632 (2007/10/02)
It was found that direct hydroxylation of aromatic rings proceeded in aqueous solution of phenyl-containing amino acids by using hydrogen-oxygen flame and that the active species of the reaction could be considered as hydroxyl radicals generated in the burning flame.
