| Autor: |
Yang Z; Department of Pathology, Stanford School of Medicine, 300 Pasteur Drive, Stanford, CA 94305, USA., Fonović M, Verhelst SH, Blum G, Bogyo M |
| Jazyk: |
angličtina |
| Zdroj: |
Bioorganic & medicinal chemistry [Bioorg Med Chem] 2009 Feb 01; Vol. 17 (3), pp. 1071-8. Date of Electronic Publication: 2008 Mar 02. |
| DOI: |
10.1016/j.bmc.2008.02.089 |
| Abstrakt: |
The field of activity-based proteomics makes use of small molecule active site probes to monitor distinct subsets of enzymatic proteins. While a number of reactive functional groups have been applied to activity-based probes (ABPs) that target diverse families of proteases, there remains a continual need for further evaluation of new probe scaffolds and reactive functional groups for use in ABPs. In this study we evaluate the utility of the, alpha,beta-unsaturated ketone reactive group for use in ABPs targeting the papain-family of cysteine proteases. We find that this reactive group shows highly selective labeling of cysteine cathepsins in both intact cells and total cell extracts. We observed a variable degree of background labeling that depended on the type of tag and linker used in the probe synthesis. The relative ease of synthesis of this class of compounds provides the potential for further derivatization to generate new families of cysteine protease ABPs with unique specificity and labeling properties. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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