AI Article Synopsis
- A new type of activity-based probes (ABPs) for metallo-aminopeptidases was developed based on the bestatin inhibitor, utilizing solid-phase synthesis for the first time.
- These ABPs effectively label metallo-aminopeptidases in an activity-dependent way, incorporating both biotin and fluorophore reporters.
- The probes are compatible with 'click' chemistry for potential applications in live cells and have demonstrated the ability to target aminopeptidases in complex proteomes, showcasing their usefulness in studying aminopeptidases in various biological contexts.
Article Abstract
A novel set of activity-based probes (ABPs) for functionally profiling metallo-aminopeptidases was synthesized based on the bestatin inhibitor scaffold, the first synthesis of bestatin analogues using solid-phase techniques. These ABPs were shown to label metallo-aminopeptidases, using both a biotin and a fluorophore reporter, in an activity-dependent manner. This probe class was also shown to be amenable to 'click' chemistry labeling for possible use in live cells. Finally, we demonstrate that the ABPs are able to label an aminopeptidase in a complex proteome. Thus, these bestatin-based probes should have wide utility to functionally profile aminopeptidases in many biological systems.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2729790 | PMC |
| http://dx.doi.org/10.1016/j.bmcl.2008.09.021 | DOI Listing |
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