Sensing
Reversible Protein–Ligand Interactions with Single-Walled Carbon Nanotube
Field-Effect Transistors
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Abstract
We
report on the reversible detection of CaptAvidin, a tyrosine
modified avidin, with single-walled carbon nanotube (SWNT) field-effect
transistors (FETs) noncovalently functionalized with biotin moieties
using 1-pyrenebutyric acid as a linker. Binding affinities at different
pH values were quantified, and the sensor’s response at various
ionic strengths was analyzed. Furthermore, protein “fingerprints”
of NeutrAvidin and streptavidin were obtained by monitoring their
adsorption at several pH values. Moreover, gold nanoparticle decorated
SWNT FETs were functionalized with biotin using 1-pyrenebutyric acid
as a linker for the CNT surface and (±)-α-lipoic acid linkers
for the gold surface, and reversible CaptAvidin binding is shown,
paving the way for potential dual mode measurements with the addition
of surface enhanced Raman spectroscopy (SERS)