Tuning the leaving group in 2-deoxy-2-fluoroglucoside results in improved activity-based retaining β-glucosidase probes

Marthe T C Walvoort; Wouter W. Kallemeijn; Lianne I. Willems; Martin D. Witte; Johannes M F G Aerts; Gijsbert A. Van Der Marel; Jeroen D C Codée; Herman S. Overkleeft

doi:10.1039/c2cc35653h

Tuning the leaving group in 2-deoxy-2-fluoroglucoside results in improved activity-based retaining β-glucosidase probes

Marthe T C Walvoort, Wouter W. Kallemeijn, Lianne I. Willems, Martin D. Witte, Johannes M F G Aerts, Gijsbert A. Van Der Marel, Jeroen D C Codée, Herman S. Overkleeft

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The potency of 2-deoxy-2-fluoroglycosides in activity-based profiling of human acid β-glucosidase is drastically improved by introducing an N-phenyl trifluoroacetimidate leaving group at the anomeric center. Protonation by the general acid-base catalyst in the active site turned out to be a prerequisite, making the imidate probe a genuine mechanism-based glycosidase inactivator.

Original language	English
Pages (from-to)	10386-10388
Number of pages	3
Journal	Chemical Communications
Volume	48
Issue number	84
DOIs	https://doi.org/10.1039/c2cc35653h
Publication status	Published - 28 Oct 2012

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title = "Tuning the leaving group in 2-deoxy-2-fluoroglucoside results in improved activity-based retaining β-glucosidase probes",

abstract = "The potency of 2-deoxy-2-fluoroglycosides in activity-based profiling of human acid β-glucosidase is drastically improved by introducing an N-phenyl trifluoroacetimidate leaving group at the anomeric center. Protonation by the general acid-base catalyst in the active site turned out to be a prerequisite, making the imidate probe a genuine mechanism-based glycosidase inactivator.",

author = "Walvoort, {Marthe T C} and Kallemeijn, {Wouter W.} and Willems, {Lianne I.} and Witte, {Martin D.} and Aerts, {Johannes M F G} and {Van Der Marel}, {Gijsbert A.} and Cod{\'e}e, {Jeroen D C} and Overkleeft, {Herman S.}",

year = "2012",

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doi = "10.1039/c2cc35653h",

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T1 - Tuning the leaving group in 2-deoxy-2-fluoroglucoside results in improved activity-based retaining β-glucosidase probes

AU - Walvoort, Marthe T C

AU - Kallemeijn, Wouter W.

AU - Willems, Lianne I.

AU - Witte, Martin D.

AU - Aerts, Johannes M F G

AU - Van Der Marel, Gijsbert A.

AU - Codée, Jeroen D C

AU - Overkleeft, Herman S.

PY - 2012/10/28

Y1 - 2012/10/28

N2 - The potency of 2-deoxy-2-fluoroglycosides in activity-based profiling of human acid β-glucosidase is drastically improved by introducing an N-phenyl trifluoroacetimidate leaving group at the anomeric center. Protonation by the general acid-base catalyst in the active site turned out to be a prerequisite, making the imidate probe a genuine mechanism-based glycosidase inactivator.

AB - The potency of 2-deoxy-2-fluoroglycosides in activity-based profiling of human acid β-glucosidase is drastically improved by introducing an N-phenyl trifluoroacetimidate leaving group at the anomeric center. Protonation by the general acid-base catalyst in the active site turned out to be a prerequisite, making the imidate probe a genuine mechanism-based glycosidase inactivator.

UR - http://www.scopus.com/inward/record.url?scp=84866895503&partnerID=8YFLogxK

U2 - 10.1039/c2cc35653h

DO - 10.1039/c2cc35653h

M3 - Article

C2 - 22932951

AN - SCOPUS:84866895503

VL - 48

SP - 10386

EP - 10388

JO - Chemical communications

JF - Chemical communications

SN - 1359-7345

IS - 84

ER -

Tuning the leaving group in 2-deoxy-2-fluoroglucoside results in improved activity-based retaining β-glucosidase probes

Abstract

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