Investigation into the inhibition of drug-metabolizing Cytochrome P450 isoenzymes by the Amazonian acai berry (Euterpe oleracea)

UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
Bradley Christopher Hollers (Creator)
Institution
The University of North Carolina at Greensboro (UNCG )
Web Site: http://library.uncg.edu/
Advisor
Gregory Raner

Abstract: Natural products, often containing a magnitude of unidentified constituents, have come under scrutiny in order to understand their effects on the human body. Cytochrome P450 enzymes, due to their non-selective nature, are highly susceptible to interference when multiple organic compounds are present in their metabolic environment. These enzymes are responsible for the oxidation of xenobiotic compounds, and thus play a crucial role in phase I drug metabolism. As part of a collaborative project at UNCG, the Amazonian acai berry (Euterpe oleracea) is being investigated for bioactive constituents based on a bioassay-guided fractionation strategy. For this study, these acai berry fractions underwent an inhibition-directed screening process against several in vitro human-model CYP450 assays. No remarkable inhibition was observed by the crude acai berry fractions for the CYP3A4 and 2D6 model assays. The 7-methoxycoumarin Odemethylation assay yielded noteworthy inhibition from chloroform-extracted acai berry constituents. Further fractionation was successfully carried out, leading to the discovery of several sub-fractions with substantial inhibition. The 78-D fraction, in particular, was found to contain the fatty acid 1-9-hexadecenoate and gave a Ki value of 73 µM. Such results give strength to the implication that a number of constituents in the acai berry could interfere with drug metabolism of one or more cytochrome P450 isoenzymes.

Additional Information

Publication
Thesis
Language: English
Date: 2014
Keywords
Acai berry, cytochrome p450, Natural products
Subjects
Ac¸ai´ palm $x Metabolism
Cytochrome P-450 $x Metabolism

Email this document to