TY - JOUR
T1 - Sensing reversible protein-ligand interactions with single-walled carbon nanotube field-effect transistors
AU - Münzer, Alexandra M.
AU - Seo, Wanji
AU - Morgan, Gregory J.
AU - Michael, Zachary P.
AU - Zhao, Yong
AU - Melzer, Katharina
AU - Scarpa, Giuseppe
AU - Star, Alexander
PY - 2014/8/7
Y1 - 2014/8/7
N2 - 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).
AB - 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).
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U2 - 10.1021/jp503670a
DO - 10.1021/jp503670a
M3 - Article
AN - SCOPUS:84905861097
SN - 1932-7447
VL - 118
SP - 17193
EP - 17199
JO - Journal of Physical Chemistry C
JF - Journal of Physical Chemistry C
IS - 31
ER -