ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022
Highly Sensitive "Off/On" EPR Probes to Monitor Enzymatic Activity.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Experimental and In Silico Approaches to Study Carboxylesterase Substrate Specificity.Journal of xenobiotics · 2026Review
- Article
- 4-Amino-TEMPO loaded liposomes as sensitive EPR and OMRI probes for the detection of phospholipase A2 activity.Scientific reports · 2023Article
- Highly Sensitive "Off/On" EPR Probes to Monitor Enzymatic Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
The assessment of unregulated level of enzyme activity is a crucial parameter for early diagnoses in a wide range of pathologies. In this study, we propose the use of electron paramagnetic resonance (EPR) as an easy method to probe carboxylesterase (CE) enzymatic activity in vitro. For this application, were synthesized two amphiphilic, nitroxide containing esters, namely Tempo-C12 (T-C12) and Tempo-2-C12 (T-2-C12). They exhibit low solubility in water and form stable micelles in which the radicals are EPR almost silent, but the hydrolysis of the ester bond yields narrows and intense EPR signals. The intensity of the EPR signals is proportional to the enzymatic activity. CEs1, CEs2 and esterase from porcine liver (PLE) were investigated. The obtained results show that T-C12 and T-2-C12-containing systems display a much higher selectivity toward the CEs2, with a Limit of Detection of the same order of those ones obtained with optical methods.
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