A radical containing micellar probe for assessing esterase enzymatic activity with ultra-low field Overhauser-enhanced magnetic resonance imaging.

Autor: Elkhanoufi S; Department of Molecular Biotechnology and Health Sciences, University of Torino, Via Nizza 52, 10126 Torino, Italy. simonetta.geninatti@unito.it., Rakhshan S; Department of Molecular Biotechnology and Health Sciences, University of Torino, Via Nizza 52, 10126 Torino, Italy. simonetta.geninatti@unito.it., Nespeca MJ; Department of Molecular Biotechnology and Health Sciences, University of Torino, Via Nizza 52, 10126 Torino, Italy. simonetta.geninatti@unito.it., Alberti D; Department of Molecular Biotechnology and Health Sciences, University of Torino, Via Nizza 52, 10126 Torino, Italy. simonetta.geninatti@unito.it., Boudries D; Magnetic Resonance Center UMR, Univ. Bordeaux, CNRS, CRMSB, UMR 5536, Case 93 146, rue Leo Saignat, F-33000 Bordeaux, France. eric.thiaudiere@rmsb.u-bordeaux.fr., Pokong-Touyam J; Magnetic Resonance Center UMR, Univ. Bordeaux, CNRS, CRMSB, UMR 5536, Case 93 146, rue Leo Saignat, F-33000 Bordeaux, France. eric.thiaudiere@rmsb.u-bordeaux.fr., Stefania R; Department of Science and Technological Innovation, University of Eastern Piedmont 'Amedeo Avogadro', Alessandria, Italy., Parzy E; Magnetic Resonance Center UMR, Univ. Bordeaux, CNRS, CRMSB, UMR 5536, Case 93 146, rue Leo Saignat, F-33000 Bordeaux, France. eric.thiaudiere@rmsb.u-bordeaux.fr., Massot P; Magnetic Resonance Center UMR, Univ. Bordeaux, CNRS, CRMSB, UMR 5536, Case 93 146, rue Leo Saignat, F-33000 Bordeaux, France. eric.thiaudiere@rmsb.u-bordeaux.fr., Mellet P; Magnetic Resonance Center UMR, Univ. Bordeaux, CNRS, CRMSB, UMR 5536, Case 93 146, rue Leo Saignat, F-33000 Bordeaux, France. eric.thiaudiere@rmsb.u-bordeaux.fr.; INSERM, Bordeaux, France., Franconi JM; INSERM, Bordeaux, France., Thiaudiere E; Magnetic Resonance Center UMR, Univ. Bordeaux, CNRS, CRMSB, UMR 5536, Case 93 146, rue Leo Saignat, F-33000 Bordeaux, France. eric.thiaudiere@rmsb.u-bordeaux.fr., Geninatti Crich S; Department of Molecular Biotechnology and Health Sciences, University of Torino, Via Nizza 52, 10126 Torino, Italy. simonetta.geninatti@unito.it.
Jazyk: angličtina
Zdroj: Journal of materials chemistry. B [J Mater Chem B] 2024 Oct 30; Vol. 12 (42), pp. 10923-10933. Date of Electronic Publication: 2024 Oct 30.
DOI: 10.1039/d4tb00639a
Abstrakt: The ability to track altered enzyme activity using a non-invasive imaging protocol is crucial for the early diagnosis of many diseases but is often challenging. Herein, we show that Overhauser magnetic resonance imaging (OMRI) can be used to monitor enzymatic conversion at an ultra-low field (206 μT) using a highly sensitive "off/on" probe with a nitroxide stable radical containing ester, named T2C 12 -T80. This TEMPO derivative containing probe forms stable electron paramagnetic resonance (EPR) silent micelles in water that are hydrolysed by esterases, thus yielding narrow EPR signals whose intensities correlate directly with specific enzymatic activity. The responsiveness of the probe to tumours, facilitated by increased esterase activity, was initially determined by comparing EPR signals measured upon incubation with 3T3 (healthy fibroblasts used as control), HepG2 (human hepatoma) and Hs766T (human pancreatic cancer cells) cell lysates and then with Hs766T and 3T3 living cells. Next, Overhauser MR images were detected on a phantom containing the probe and the esterases to show that the approach is well suited for being translated to the in vivo detection at the earth's magnetic field. Regarding detection sensitivity, ultra-low field OMRI (ULF-OMRI) is beneficial over OMRI at higher fields ( e.g. 0.2 T) since Overhauser enhancements are significantly higher and the technique is safe in terms of the specific absorption rate.
Databáze: MEDLINE
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