Published on : Sep 10, 2014
The findings of a certain study that have been published in the journal Chemistry and Biology discusses a mechanism that inhibits the growth of cancer targeting protein complexes known as proteasomes. The research study was first authored by Daniela Trivella who is a researcher at the Brazilian Biosciences National Laboratory at the Brazilian Center for Research in Energy and Materials (LNBio/CNPEM).
This research study was conducted with the support of the FAPESP which included the partnership of researchers from Germany’s Technische Universitat Munchen and researchers from the University of California located in San Diego. The main rationale of this research team is to develop a new genesis of cancer drugs that are less toxic and more effective.
A new series of molecules have already been developed which are based on the new found mechanism. The primary aim is to optimize the inhibition effect of proteasomes thereby making the product even more selective of tumor cells and reduce the problem of resistance of the drugs currently available in the market.
Proteasomes, which is a member of Proteases, a category of enzymes is responsible for carrying out several vital functions like cell division, elimination of harmful proteins, and regulation of apoptosis.
A very potent and effective inhibitor of proteasomes is Epoxyketones which interact with the enzymes in two phases. In order to optimize the effects of Epoxyketones and discover new reactive groups the researchers at the University of California have developed a set of synthetic analogs with a few minor structural modifications. One molecule had features of carmaphycin and contained an enone as a reactive group and the other molecule that was isolated from plant pathogens contained syringolin. The researchers also observed that the new molecule, just like epoxyketone interacted with the proteasomes in two stages.
Toxicity tests are there in the pipeline however, studies conducted with the help of crystallography procedures have shown the way in which interaction occurs between the carmaphycin-syringolin enone and the target enzyme.