Bisphosphonate ligand mediated ultrasensitive capacitive protein sensor: complementary match of supramolecular and dynamic chemistry. (10th December 2018)

• Record Type: Journal Article
• Authors: Ertürk, Gizem; Akhoundian, Maedeh; Lueg-Althoff, Kyra; Shinde, Sudhirkumar; Yeung, Sing Yee; Hedström, Martin; Schrader, Thomas; Mattiasson, Bo; Sellergren, Börje
• Is Part Of: New journal of chemistry. Volume 43:Number 2(2019)
• Page Start: 847
• Page End: 852
• Publication Date: 2018-12-10
• Subjects: Chemistry -- Periodicals; Chimie -- Périodiques; 540
• DOI: 10.1039/c8nj05238g
• Languages: English
• ISSNs: 1144-0546

Abstract

Abstract : A powerful polymeric protein sensor was constructed by microcontact imprinting taking advantage of the specific interaction between a bisphosphonate binding monomer and lysine/arginine residues on the surface of trypsin. Abstract : Modern healthcare demands rapid and accurate detection of proteins/enzymes at the ultratrace level. Herein we present a molecularly imprinted capacitive sensor for trypsin, developed by microcontact imprinting. High affinity and selectivity was achieved by doping the prepolymerization mixture with a stoichiometric amount of methacrylamide-based bisphosphonate (BP) monomer. Taking advantage of the specific interaction between bisphosphonate binding monomers and lysine/arginine residues on the surface of trypsin, we have constructed a powerful polymeric sensor. The BP based sensor has the ability to recognize trypsin over other arginine-rich proteins, even in high ionic strength buffers with a sub-picomolar detection limit (pM). We believe that the combination of supramolecular chemistry, molecular imprinting and advanced instrumentation has a potential for future drug development and diagnostics that extends beyond biomolecular recognition.