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  • Petrosamine B, an Inhibitor of the Helicobacter pylori Enzyme Aspartyl Semialdehyde Dehydrogenase from the Australian Sponge Oceanapia sp.

    Author(s)
    Carroll, AR
    Ngo, A
    Quinn, RJ
    Redburn, J
    Hooper, JNA
    Griffith University Author(s)
    Quinn, Ronald J.
    Redburn, Joanne
    Carroll, Anthony R.
    Ngo, Anna
    Hooper, John N.
    Year published
    2005
    Metadata
    Show full item record
    Abstract
    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 卮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 卮
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    Journal Title
    Journal of Natural Products
    Volume
    68
    Issue
    5
    Publisher URI
    http://pubs.acs.org/journal/jnprdf
    DOI
    https://doi.org/10.1021/np049595s
    Copyright Statement
    © 2005 American Chemical Society. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please use the hypertext link above to access the journal's website or contact the author for more information.
    Subject
    Chemical Sciences
    Biological Sciences
    Medical and Health Sciences
    Publication URI
    http://hdl.handle.net/10072/4169
    Collection
    • Journal articles

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