Fiche publication
Date publication
juin 2024
Journal
Advanced science (Weinheim, Baden-Wurttemberg, Germany)
Auteurs
Membres identifiés du Cancéropôle Est :
Dr MONCHAUD David
Tous les auteurs :
Qiu D, He F, Liu Y, Zhou Z, Yang Y, Long Z, Chen Q, Chen D, Wei S, Mao X, Zhang X, Mergny JL, Monchaud D, Ju H, Zhou J
Lien Pubmed
Résumé
Nanomaterials excel in mimicking the structure and function of natural enzymes while being far more interesting in terms of structural stability, functional versatility, recyclability, and large-scale preparation. Herein, the story assembles hemin, histidine analogs, and G-quadruplex DNA in a catalytically competent supramolecular assembly referred to as assembly-activated hemin enzyme (AA-heminzyme). The catalytic properties of AA-heminzyme are investigated both in silico (by molecular docking and quantum chemical calculations) and in vitro (notably through a systematic comparison with its natural counterpart horseradish peroxidase, HRP). It is found that this artificial system is not only as efficient as HRP to oxidize various substrates (with a turnover number k of 115 s) but also more practically convenient (displaying better thermal stability, recoverability, and editability) and more economically viable, with a catalytic cost amounting to <10% of that of HRP. The strategic interest of AA-heminzyme is further demonstrated for both industrial wastewater remediation and biomarker detection (notably glutathione, for which the cost is decreased by 98% as compared to commercial kits).
Mots clés
G‐quadruplex, artificial enzyme, hemin, histidine analogs
Référence
Adv Sci (Weinh). 2024 06 25;:e2402237
