2022
Non-psychotropic cannabinoids as inhibitors of TET1 protein
ANTONYOVÁ, Veronika; Zdeněk KEJÍK; Tereza BROGYANYI; Robert KAPLÁNEK; Kateřina VESELÁ et al.Základní údaje
Originální název
Non-psychotropic cannabinoids as inhibitors of TET1 protein
Autoři
ANTONYOVÁ, Veronika; Zdeněk KEJÍK; Tereza BROGYANYI; Robert KAPLÁNEK; Kateřina VESELÁ; Nikita ABRAMENKO; Tomáš OCELKA; Michal MASAŘÍK; Adam MATKOWSKI; Jakub GBUREK; Renata ABEL; Andrean GOEDE; Robert PREISSNER; Petr NOVOTNÝ a Milan JAKUBEK
Vydání
Bioorganic Chemistry, San Dieo, ACADEMIC PRESS INC ELSEVIER SCIENCE, 2022, 0045-2068
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
30105 Physiology
Stát vydavatele
Slovinsko
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 5.100
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14110/22:00125768
Organizační jednotka
Lékařská fakulta
UT WoS
EID Scopus
Klíčová slova anglicky
Cannabinoids; TET1 protein; Iron chelation; DNA methylation; Epigenetic
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 19. 7. 2022 10:51, Mgr. Tereza Miškechová
Anotace
V originále
Non-psychotropic cannabinoids (e.g., cannabidiol, cannabinol and cannabigerol) are contained in numerous alimentary and medicinal products. Therefore, predicting and studying their possible side effects, such as changes in DNA methylation, is an important task for assessing the safety of these products. Interference with TET enzymes by chelating ferrous ions can contribute to the altered methylation pattern. All tested cannabinoids displayed a strong affinity for Fe(II) ions. Cannabidiol and cannabinol exhibited potent inhibitory activities (IC50 = 4.8 and 6.27 μM, respectively) towards the TET1 protein, whereas cannabigerol had no effect on the enzyme activity. An in silico molecular docking study revealed marked binding potential within the catalytic cavity for CBD/CBN, but some affinity was also found for CBG, thus the total lack of activity remains unexplained. These results imply that cannabinoids could affect the activity of the TET1 protein not only due to their affinity for Fe(II) but also due to other types of interactions (e.g., hydrophobic interactions and hydrogen bonding).
Návaznosti
| LM2018133, projekt VaV |
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| NU21-08-00407, projekt VaV |
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| TN01000013, projekt VaV |
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