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Updated: Jun 30, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
Published on: July 25, 2013
The inhibition of protein phosphatases 1 and 2A: a new target for rational anti-cancer drug design?
A McCluskey1, S P Ackland, E Gardiner
1Medicinal Chemistry Group, School of Environmental and Life Sciences, The University of Newcastle, NSW, Australia. amcclusk@mail.newcastle.edu.au
Abstract:
Recent investigations in our laboratories have highlighted that the inhibition of the serine/threonine protein phosphatases 1 and 2A (PP1 and PP2A) is an excellent target for the development of novel anti-cancer agents. Using a combination of the known crystal structure of PP1 and the modelled structure of PP2A, we have rationally designed a new class of protein phosphatase inhibitors, cantharimides, which exhibit broad-spectrum anti-cancer activity. Synthetic modifications of the simplest known PP1 and PP2A inhibitor, norcantharidin, has led to the development of potent PP1 and PP2A inhibitors.
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