Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases. Issue 3 (28th July 2020)

• Record Type: Journal Article
• Authors: de Boer, Casper; McGregor, Nicholas G. S.; Peterse, Evert; Schröder, Sybrin P.; Florea, Bogdan I.; Jiang, Jianbing; Reijngoud, Jos; Ram, Arthur F. J.; van Wezel, Gilles P.; van der Marel, Gijsbert A.; Codée, Jeroen D. C.; Overkleeft, Herman S.; Davies, Gideon J.
• Is Part Of: RSC chemical biology. Volume 1: Issue 3(2020)
• Page Start: 148
• Page End: 155
• Publication Date: 2020-07-28
• Subjects: 572
• DOI: 10.1039/d0cb00045k
• Languages: English
• ISSNs: 2633-0679

Abstract

Abstract : New cyclophellitol-derived activity-based probes enable the sensitive detection and identification of cellulases. Abstract : Cellulases and related β-1, 4-glucanases are essential components of lignocellulose-degrading enzyme mixtures. The detection of β-1, 4-glucanase activity typically relies on monitoring the breakdown of purified lignocellulose-derived substrates or synthetic chromogenic substrates, limiting the activities which can be detected and complicating the tracing of activity back to specific components within complex enzyme mixtures. As a tool for the rapid detection and identification of β-1, 4-glucanases, a series of glycosylated cyclophellitol inhibitors mimicking β-1, 4-glucan oligosaccharides have been synthesised. These compounds are highly efficient inhibitors of HiCel7B, a well-known GH7 endo -β-1, 4-glucanase. An elaborated activity-based probe facilitated the direct detection and identification of β-1, 4-glucanases within a complex fungal secretome without any detectable cross-reactivity with β-d -glucosidases. These probes and inhibitors add valuable new capacity to the growing toolbox of cyclophellitol-derived probes for the activity-based profiling of biomass-degrading enzymes.