Bisphosphonate ligand mediated ultrasensitive capacitive protein sensor: complementary match of supramolecular and dynamic chemistry

Gizem Ertürk, Maedeh Akhoundian, Kyra Lueg-Althoff, Sudhirkumar Shinde, Sing Yee Yeung, Martin Hedström, Thomas Schrader, Bo Mattiasson, Börje Sellergren

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.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.
Original languageEnglish
Pages (from-to)847-852
Number of pages6
JournalNew journal of chemistry
Volume43
Issue number2
Early online date04 Dec 2018
DOIs
Publication statusPublished - 14 Jan 2019

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