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On the Possible Effect of Phytic Acid (Myo-Inositol Hexaphosphoric Acid, IP6) on Cytochromes P450 and Systems of Xenobiotic Metabolism in Different Hepatic Models

V. Frybortova, S. Satka, L. Jourova, I. Zapletalova, M. Srejber, P. Briolotti, M. Daujat-Chavanieu, S. Gerbal-Chaloin, P. Anzenbacher, M. Otyepka, E. Anzenbacherova

. 2024 ; 25 (7) : . [pub] 20240323

Jazyk angličtina Země Švýcarsko

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc24014544

Grantová podpora
RVO 61989592 Palacký University, Olomouc
IGA_LF_2024_006 Palacký University, Olomouc
IGA_LF_2024_011 Palacký University, Olomouc
e-INFRA CZ project no. ID:90254 Ministry of Education, Youth and Sports of the Czech Republic

As compounds of natural origin enter human body, it is necessary to investigate their possible interactions with the metabolism of drugs and xenobiotics in general, namely with the cytochrome P450 (CYP) system. Phytic acid (myo-inositol hexaphosphoric acid, IP6) is mainly present in plants but is also an endogenous compound present in mammalian cells and tissues. It has been shown to exhibit protective effect in many pathological conditions. For this paper, its interaction with CYPs was studied using human liver microsomes, primary human hepatocytes, the HepG2 cell line, and molecular docking. Docking experiments and absorption spectra demonstrated the weak ability of IP6 to interact in the heme active site of CYP1A. Molecular docking suggested that IP6 preferentially binds to the protein surface, whereas binding to the active site of CYP1A2 was found to be less probable. Subsequently, we investigated the ability of IP6 to modulate the metabolism of xenobiotics for both the mRNA expression and enzymatic activity of CYP1A enzymes. Our findings revealed that IP6 can slightly modulate the mRNA levels and enzyme activity of CYP1A. However, thanks to the relatively weak interactions of IP6 with CYPs, the chances of the mechanisms of clinically important drug-drug interactions involving IP6 are low.

Citace poskytuje Crossref.org

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