Abstract
Previously, it was suggested that the natural compound curcumin is an irreversible inhibitor of rhodesain, the major lysosomal cysteine protease of the protozoan parasite Trypanosoma brucei. The suggestion was based on a time-dependent inhibition of the enzyme by curcumin and a lack of recovery of activity of the enzyme after pre-incubation with curcumin. This study provides clear evidence that curcumin is a reversible, non-competitive inhibitor of rhodesain. In addition, the study also shows that the apparent irreversible inhibition of curcumin is only observed when no thiol-reducing reagent is included in the measuring buffer and insufficient solubilising agent is added to fully dissolve curcumin in the aqueous solution. Thus, the previous observation that curcumin acts as an irreversible inhibitor for rhodesain was based on a misinterpretation of experimental findings.
Highlights
Curcumin is a natural phenol and has been extensively investigated as potential drug candidate for various illnesses and medical conditions [1]
In search for the biological target involved in the trypanocidal activity of curcumin, the effect of the compound on rhodesain, the major lysosomal cathepsin L cysteine protease in T. brucei, has been recently investigated [3]
The results of this study revealed that curcumin is a reversible non‐competitive inhibitor of rhodesain,unequivocally a new finding that disproves claims that curcumin an disproves previous claims thatunequivocally curcumin is anprevious irreversible inhibitor
Summary
Curcumin is a natural phenol and has been extensively investigated as potential drug candidate for various illnesses and medical conditions [1]. PAINS are compounds that show activity in different types of assay mainly through interfering with the assay itself while IMPS are reagents that display activity against virtually any biological target. Despite this and other drawbacks (chemical instability, low bioavailability, non-selectivity and toxicity), curcumin is still subject of intense research and about 50 papers are published each week on biological interactions of the compound [1]. The results of this study revealed that curcumin is a reversible non-competitive inhibitor of rhodesain, a new finding that
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
