Related Experiment Video
Updated: Jun 9, 2026
Automated System for Single Molecule Fluorescence Measurements of Surface-immobilized Biomolecules
Published on: November 2, 2009
Pharmacophore-targeted fluorescence sensing of ibrutinib via Michael addition-induced electron transfer on
Mohamed N Goda1, Laila S Alqarni1, Faisal K Algethami1
1Department of Chemistry, College of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU) Riyadh 11623 Saudi Arabia.
Ibrutinib (IBR), an irreversible inhibitor of Bruton's tyrosine kinase, is commonly used as a first-line therapy for chronic lymphocytic leukemia (CLL) and various other B-cell cancers. Given its narrow therapeutic window and the clinical necessity of long-term administration, accurate therapeutic drug monitoring of IBR in biological fluids is of paramount importance. Herein, we report a novel fluorometric sensing platform for the selective and sensitive determination of IBR based on thiol-functionalized carbon dots (HS-CDs). The sensing mechanism relies on the specific covalent interaction between the -SH groups on HS-CDs and the electrophilic acrylamide moiety of IBR through a rapid Michael addition reaction, which anchors IBR to the CD surface. This binding modifies the local electronic environment of the carbon dots and promotes efficient electron interaction between the electron-rich nitrogen-containing groups of IBR and the CD fluorophore, collectively leading to a concentration-dependent enhancement of fluorescence. The sensor, under optimized conditions, responded linearly from 1.0 to 30.0 ng mL-1, with a minimum detectable concentration of 0.21 ng mL-1. The practical applicability of the platform was demonstrated through the direct quantification of IBR in human serum samples collected from CLL patients, achieving satisfactory recovery values (97.0-100.2%) with minimal sample preparation. The proposed method has strong potential for routine therapeutic drug monitoring in CLL patients undergoing ibrutinib therapy.
Ibrutinib (IBR), an irreversible inhibitor of Bruton's tyrosine kinase, is commonly used as a first-line therapy for chronic lymphocytic leukemia (CLL) and various other B-cell cancers. Given its narrow therapeutic window and the clinical necessity of long-term administration, accurate therapeutic drug monitoring of IBR in biological fluids is of paramount importance. Herein, we report a novel fluorometric sensing platform for the selective and sensitive determination of IBR based on thiol-functionalized carbon dots (HS-CDs). The sensing mechanism relies on the specific covalent interaction between the -SH groups on HS-CDs and the electrophilic acrylamide moiety of IBR through a rapid Michael addition reaction, which anchors IBR to the CD surface. This binding modifies the local electronic environment of the carbon dots and promotes efficient electron interaction between the electron-rich nitrogen-containing groups of IBR and the CD fluorophore, collectively leading to a concentration-dependent enhancement of fluorescence. The sensor, under optimized conditions, responded linearly from 1.0 to 30.0 ng mL-1, with a minimum detectable concentration of 0.21 ng mL-1. The practical applicability of the platform was demonstrated through the direct quantification of IBR in human serum samples collected from CLL patients, achieving satisfactory recovery values (97.0-100.2%) with minimal sample preparation. The proposed method has strong potential for routine therapeutic drug monitoring in CLL patients undergoing ibrutinib therapy.
