Different approaches to label biomolecules have been developed in the last years, including bioorthogonal chemical reactions such as cycloaddition, photoactivation together with enzymatic labelling.1 The aim of this project is to use an enzymatic process : the myrosinase-glucosinolate (MG) reaction as a bioconjugation tool. This enzymatic reaction occurs in the Brassicales plants order, in which the thioglucosidase myrosinase, hydrolyzes secondary metabolites, glucosinolates (GLs) into isothiocyanates (ITCs).2 As strong electrophile, the ITCs are well known and useful in bioconjugation, but are toxic, not easy to prepare and to store. The advantage of this enzymatic reaction would be to generate ITCs from a stable, non-toxic, water soluble GL precursor (Figure 1). To begin, mannose specific lectins as Concanavalin A and the E. coli bacterial fimbrial adhesin FimH were carefully chosen as biological targets.3 Therefore, GLs bearing a lectin ligand moiety, were developed in order to set up a new tool for site selective bioconjugation or protein functionalization. We will disclose our recent results on the design and the reactivity of novel artificial GLs together with the MG system utilization in bioconjugate chemistry.4

Myrosinase–glucosinolate system: Enzymatic triggered isothiocyanate for bioconjugate chemistry

2019 Fall National Meeting

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