2812-32-0Relevant articles and documents
Pagoamide A, a Cyclic Depsipeptide Isolated from a Cultured Marine Chlorophyte, Derbesia sp., Using MS/MS-Based Molecular Networking
Cottrell, Garrison W.,Fang, Fang,Gerwick, Lena,Gerwick, William H.,Glukhov, Evgenia,Guan, Huashi,Kim, Hyunwoo,Leao, Tiago,Li, Yueying,Mao, Huanru Henry,Murray, Thomas F.,Pierce, Marsha L.,Yu, Hao-Bing,Zhang, Chen,Zhang, Yi
supporting information, (2020/01/31)
A thiazole-containing cyclic depsipeptide with 11 amino acid residues, named pagoamide A (1), was isolated from laboratory cultures of a marine Chlorophyte, Derbesia sp. This green algal sample was collected from America Samoa, and pagoamide A was isolated using guidance by MS/MS-based molecular networking. Cultures were grown in a light- and temperature-controlled environment and harvested after several months of growth. The planar structure of pagoamide A (1) was characterized by detailed 1D and 2D NMR experiments along with MS and UV analysis. The absolute configurations of its amino acid residues were determined by advanced Marfey's analysis following chemical hydrolysis and hydrazinolysis reactions. Two of the residues in pagoamide A (1), phenylalanine and serine, each occurred twice in the molecule, once in the d- and once in the l-configuration. The biosynthetic origin of pagoamide A (1) was considered in light of other natural products investigations with coenocytic green algae.
Caldoramide, a Modified Pentapeptide from the Marine Cyanobacterium Caldora penicillata
Gunasekera, Sarath P.,Imperial, Lorelie,Garst, Christiana,Ratnayake, Ranjala,Dang, Long H.,Paul, Valerie J.,Luesch, Hendrik
, p. 1867 - 1871 (2016/08/02)
The isolation, structure determination, and biological activities of a new linear pentapeptide, caldoramide (5), from the marine cyanobacterium Caldora penicillata from Florida are described. Caldoramide (5) has structural similarities to belamide A (4), dolastatin 10 (1), and dolastatin 15 (2). We profiled caldoramide against parental HCT116 colorectal cancer cells and isogenic cells lacking oncogenic KRAS or hypoxia-inducible factors 1α (HIF-1α) and 2α (HIF-2α). Caldoramide (5) showed differential cytotoxicity for cells containing both oncogenic KRAS and HIF over the corresponding knockout cells. LCMS dereplication indicated the presence of caldoramide (5) in a subset of C. penicillata samples.
Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation
Kwan, Jason C.,Eksioglu, Erika A.,Liu, Chen,Paul, Valerie J.,Luesch, Hendrik
experimental part, p. 5732 - 5747 (2010/03/24)
In our efforts to exploremarine cyanobacteria as a source of novel bioactive compounds, we discovered a statine unit-containing linear decadepsipeptide, grassystatin A (1), which we screened against a diverse set of 59 proteases. We describe the structure