Petrosamine B, an Inhibitor of the Helicobacter pylori Enzyme Aspartyl Semialdehyde Dehydrogenase from the Australian Sponge Oceanapia sp
Autor: | Ronald J. Quinn, Anna Ngo, Anthony R. Carroll, John N. A. Hooper, Joanne Redburn |
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Rok vydání: | 2005 |
Předmět: |
Stereochemistry
Aspartate-semialdehyde dehydrogenase Pharmaceutical Science Dehydrogenase Analytical Chemistry Inhibitory Concentration 50 Alkaloids Bacterial Proteins Drug Discovery Animals Enzyme Inhibitors Antibacterial agent Pharmacology chemistry.chemical_classification Helicobacter pylori Molecular Structure biology Chemistry Alkaloid Organic Chemistry Australia Biological activity Aldehyde Dehydrogenase Phenanthrenes Porifera Enzyme Complementary and alternative medicine Biochemistry Enzyme inhibitor biology.protein Acridines Molecular Medicine Antibacterial activity |
Zdroj: | Journal of Natural Products. 68:804-806 |
ISSN: | 1520-6025 0163-3864 |
DOI: | 10.1021/np049595s |
Popis: | Bioassay-guided fractionation of the MeOH extract of the sponge Oceanapia sp. using the Helicobacter pylori enzyme, aspartyl semialdehyde dehydrogenase, ASD, to detect antibacterial activity, led to the isolation of a new pyridoacridine alkaloid, petrosamine B (1). Petrosamine B is a bright blue compound that is sparingly soluble in many organic solvents. The structure of 1 was determined from detailed NMR studies performed in TFA/D2O. Petrosamine B was found to be a weak inhibitor of ASD with an IC50 of 306 microM. |
Databáze: | OpenAIRE |
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