Research output: Contribution to journal › Article › peer-review
Journal | Journal of the American Chemical Society |
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Date | E-pub ahead of print - 8 Aug 2014 |
Issue number | 33 |
Volume | 136 |
Number of pages | 4 |
Pages (from-to) | 11622-11625 |
Original language | English |
Lysosomal degradation of glycosphingolipids is mediated by the consecutive action of several glycosidases. Malfunctioning of one of these hydrolases can lead to a lysosomal storage disorder such as Fabry disease, which is caused by a deficiency in α-galactosidase A. Herein we describe the development of potent and selective activity-based probes that target retaining α-galactosidases. The fluorescently labeled aziridine-based probes 3 and 4 inhibit the two human retaining α-galactosidases αGal A and αGal B covalently and with high affinity. Moreover, they enable the visualization of the endogenous activity of both α-galactosidases in cell extracts, thereby providing a means to study the presence and location of active enzyme levels in different cell types, such as healthy cells versus those derived from Fabry patients.
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