HOT: potentially toxic interaction of AAP and catalase – a protocol for characterising drug-enzyme mechanisms

4-aminoantipyrine (AAP) has analgesic, antipyretic and anti-inflammatory properties but is rarely used therapeutically because of serious side effects, including lowered white blood cell counts.  However, it is widely used in the pharmaceutical industry as a raw material, in biochemical research and in environmental monitoring studies to detect phenols in the environment.  In order to investigate some of its toxic side effects, Rutao Liu et al. from Shandong University have investigated how it binds to catalase, an important antioxidant enzyme.

Their protocol entails the use of molecular docking and spectroscopic methods, including UV-visible absorption, synchronous fluorescence and circular dichroism to provide detailed information on binding of AAP to catalase and the conformational and microenvironmental changes that result from the binding event.

Their results show that exposure to AAP could induce changes in the enzyme structure and function, and the authors hope the methods in this work can be applied to characterize interactions of enzyme systems and other pollutants and drugs.

Molecular interaction between 4-aminoantipyrine and catalase reveals a potentially toxic mechanism of the drug
Yue Teng, Hao Zhang and Rutao Liu
Mol. BioSyst., 2011, Advance Article
DOI: 10.1039/C1MB05271C

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