Tuning probe selectivity for chemical proteomics applications

Subfamily-Specific Fluorescent Probes for Cysteine Proteases Display Dynamic Protease Activities during Seed Germination

“…Protease activity profiling (also called activity-based protein profiling of proteases) is an easy and powerful method to monitor the active state of proteases in crude extracts or living organisms (Heal et al, 2011;Serim et al, 2012;Haedke et al, 2013;Willems et al, 2014). Protease activity profiling is based on the use of chemical probes that react covalently with the active site of proteases in an activitydependent manner.…”

Comparative Analysis of Click Chemistry Mediated Activity-Based Protein Profiling in Cell Lysates

“…The introduction of covalent small molecule probes can be based on different types of chemistries: probes may be incorporated by the use of exogenous or endogenous enzymes [1,2], or they can contain an intrinsic reactivity such as an electrophile or photocrosslinker that by itself forms a covalent bond to the target proteins [3,4,5]. Generally, the probes can be dramatically adjusted in their selectivity by a combination of the reactive groups and additional structural elements that interact with the target proteins [6]. Activity-based protein profiling (ABPP) is a particularly interesting method, since it is able to address the functional state of a protein, i.e.…”

Structural Chemistry of Basic Magnesium Acetates, Mg5(μ3‐OH)2(OAc)8·nL and Mg3(μ4‐O)(OAc)4

“…Due to the expanding applicability of ABPs in profiling, imaging and inhibitor screening methods,3 quick synthetic access to ABPs is crucial. Furthermore, some applications require the ability to tune the ABP selectivity towards a specific subset of enzymes or even a single enzyme 4. To achieve both rapid synthesis and probe optimization, solid‐phase synthesis has been successfully applied in the construction of ABPs for cysteine proteases,5–7 the proteasome,8 and tyrosine phosphatases,9 for example.…”