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. 2022 Jan 18;12(2):90. doi: 10.3390/metabo12020090

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Two-dimensional diagram of (A). Most active compound: Quercetin 3-O-ß-D-2″-acetylglucuronide methyl ester (related to docking binding energy) and its main interactions into the acetylcholinesterase (TcAChE) catalytic site. (B). Most active compound: Quercetin 3-O-(ß-D-glucuronide) (related to docking binding energy) and its main interactions into the butyrylcholinesterase (hBuChE) catalytic site. (C). Most active compound: Quercetin 3-O-ß D-2″-acetylglucuronide (related to docking binding energy) and its main interactions into the tyrosinase catalytic site. Purple arrows represents hydrogen bond interactions, green lines represents π-π interactions and red lines represents π-cation interactions.

Two-dimensional diagram of (A). Most active compound: Quercetin 3-O-ß-D-2″-acetylglucuronide methyl ester (related to docking binding energy) and its main interactions into the acetylcholinesterase (TcAChE) catalytic site. (B). Most active compound: Quercetin 3-O-(ß-D-glucuronide) (related to docking binding energy) and its main interactions into the butyrylcholinesterase (hBuChE) catalytic site. (C). Most active compound: Quercetin 3-O-ß D-2″-acetylglucuronide (related to docking binding energy) and its main interactions into the tyrosinase catalytic site. Purple arrows represents hydrogen bond interactions, green lines represents π-π interactions and red lines represents π-cation interactions.