| 1. |
- Bergdahl, Gizem Ertürk, et al.
(författare)
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Bisphosphonate Ligand Mediated Ultrasensitive Capacitive Protein Sensor : Complementary Match of Supramolecular and Dynamic Chemistry
- 2019
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Ingår i: New Journal of Chemistry. - : Royal Society of Chemistry. - 1144-0546 .- 1369-9261. ; 43:2, s. 847-852
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Tidskriftsartikel (refereegranskat)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 strong interaction of bisphosphonate with 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.
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| 2. |
- Ertürk, Gizem, et al.
(författare)
-
Bisphosphonate ligand mediated ultrasensitive capacitive protein sensor : complementary match of supramolecular and dynamic chemistry
- 2018
-
Ingår i: New Journal of Chemistry. - : Royal Society of Chemistry (RSC). - 1144-0546 .- 1369-9261. ; 43:2, s. 847-852
-
Tidskriftsartikel (refereegranskat)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.
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