1108702-33-5Relevant 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 (2012/03/27)
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.