JAKUBEK, Milan, Michal MASAŘÍK, Tomas BRIZA, Robert KAPLANEK, Katerina VESELA, Nikita ABRAMENKO and Pavel MARTASEK. PPO-Inhibiting Herbicides and Structurally Relevant Schiff Bases: Evaluation of Inhibitory Activities against Human Protoporphyrinogen Oxidase. Processes. Basel: MDPI, 2021, vol. 9, No 2, p. 1-16. ISSN 2227-9717. Available from: https://dx.doi.org/10.3390/pr9020383.
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Basic information
Original name PPO-Inhibiting Herbicides and Structurally Relevant Schiff Bases: Evaluation of Inhibitory Activities against Human Protoporphyrinogen Oxidase
Authors JAKUBEK, Milan (203 Czech Republic), Michal MASAŘÍK (203 Czech Republic, belonging to the institution), Tomas BRIZA (203 Czech Republic), Robert KAPLANEK (203 Czech Republic), Katerina VESELA (203 Czech Republic), Nikita ABRAMENKO and Pavel MARTASEK (203 Czech Republic).
Edition Processes, Basel, MDPI, 2021, 2227-9717.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 20402 Chemical process engineering
Country of publisher Switzerland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 3.352
RIV identification code RIV/00216224:14110/21:00121763
Organization unit Faculty of Medicine
Doi http://dx.doi.org/10.3390/pr9020383
UT WoS 000623166400001
Keywords in English protoporphyrinogen oxidase; inhibitors; herbicides
Tags 14110515, 14110518, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Tereza Miškechová, učo 341652. Changed: 21/3/2022 07:54.
Abstract
The study of human protoporphyrinogen oxidase (hPPO) inhibition can contribute significantly to a better understanding of some pathogeneses (e.g., porphyria, herbicide exposure) and the development of anticancer agents. Therefore, we prepared new potential inhibitors with Schiff base structural motifs (2-hydroxybenzaldehyde-based Schiff bases 9-13 and chromanone derivatives 17-19) as structurally relevant to PPO herbicides. The inhibitory activities (represented by the half maximal inhibitory concentration (IC50) values) and enzymatic interactions (represented by the hPPO melting temperatures) of these synthetic compounds and commercial PPO herbicides used against hPPO were studied by a protoporphyrin IX fluorescence assay. In the case of PPO herbicides, significant hPPO inhibition and changes in melting temperature were observed for oxyfluorten, oxadiazon, lactofen, butafenacil, saflufenacil, oxadiargyl, chlornitrofen, and especially fomesafen. Nevertheless, the prepared compounds did not display significant inhibitory activity or changes in the hPPO melting temperature. However, a designed model of hPPO inhibitors based on the determined IC50 values and a docking study (by using AutoDock) found important parts of the herbicide structural motif for hPPO inhibition. This model could be used to better predict PPO herbicidal toxicity and improve the design of synthetic inhibitors.
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