Lucanthone and Hycanthone Inhibit APE1 by Direct Protein Binding
Author Information
Author(s): Naidu Mamta D., Agarwal Rakhi, Pena Louis A., Cunha Luis, Mezei Mihaly, Shen Min, Wilson David M. III, Liu Yuan, Sanchez Zina, Chaudhary Pankaj, Wilson Samuel H., Waring Michael J.
Primary Institution: Brookhaven National Laboratory
Hypothesis
Hydrophobic molecules like lucanthone and hycanthone inhibit APE1 by binding to its hydrophobic pocket.
Conclusion
Lucanthone and hycanthone inhibit APE1 endonuclease activity primarily through direct interaction rather than by affecting its DNA binding capacity.
Supporting Evidence
- Lucanthone inhibits APE1 endonuclease activity without affecting its redox function.
- The binding affinity of hycanthone to APE1 is significantly higher than that of lucanthone.
- Lucanthone and hycanthone induce conformational changes in APE1.
Takeaway
Lucanthone and hycanthone are drugs that can stop a protein called APE1 from working properly, which might help treat certain cancers.
Methodology
The study involved biochemical assays, molecular docking, and binding studies to analyze the interaction between APE1 and the inhibitors.
Limitations
The study primarily focused on in vitro experiments, which may not fully represent in vivo conditions.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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