Inhibition of human vascular NADPH oxidase by apocynin derived oligophenols
Authors
Mora-Pale, M.
Weïwer, M.
Yu, J.
Linhardt, Robert J.
Dordick, J.S.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2009-07-15
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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Full Citation
Inhibition of human vascular NADPH oxidase by apocynin derived oligophenols, M. Mora-Pale, M. Weïwer, J. Yu, R.J. Linhardt, J.S. Dordick, Bioorganic Chemistry and Medicinal Chemistry, 17, 5146–5152, 2009.
Abstract
Enzymatic oxidation of apocynin, which may mimic in vivo metabolism, affords a large number of oligomers (apocynin oxidation products, AOP) that inhibit vascular NADPH oxidase. In vitro studies of NADPH oxidase activity were performed to identify active inhibitors, resulting in a trimer hydroxylated quinone (IIIHyQ) that inhibited NADPH oxidase with an IC50 = 31 nM. Apocynin itself possessed minimal inhibitory activity. NADPH oxidase is believed to be inhibited through prevention of the interaction between two NADPH oxidase subunits, p47phox and p22phox. To that end, while apocynin was unable to block the interaction of his-tagged p47phox with a surface immobilized biotinalyted p22phox peptide, the IIIHyQ product strongly interfered with this interaction (apparent IC50 = 1.6 μM). These results provide evidence that peroxidase-catalyzed AOP, which consist of oligomeric phenols and quinones, inhibit critical interactions that are involved in the assembly and activation of human vascular NADPH oxidase.
Description
Bioorganic Chemistry and Medicinal Chemistry, 17, 5146–5152
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Elsevier
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Bioorganic and Medicinal Chemistry
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
Bioorganic and Medicinal Chemistry
https://harc.rpi.edu/
Access
A full text version is available in DSpace@RPI