TY - JOUR
T1 - Selective antigen-antibody recognition on SPR sensor based on the heat-sensitive conformational change of poly(N-isopropylacrylamide)
AU - Song, Seung Yeon
AU - Choi, Hyoung Gil
AU - Hong, Jung Woo
AU - Kim, Byung Woo
AU - Sim, Sang Jun
AU - Yoon, Hyun C.
N1 - Funding Information:
This research was supported by grants from Center for Nanoscale Mechatronics & Manufacturing (MOST) and the Basic Research Program of KOSEF (R01-2006-000-10240-0).
PY - 2008/2/1
Y1 - 2008/2/1
N2 - We describe the modulation of biointerface by an external stimulus with a smart polymer-modified electrode. Poly(N-isopropylacrylamide) (PNIPAAm) shows a rapid reversible hydrophilic/hydrophobic transition of its conformation in response to the temperature variation across its lower critical solution temperature (LCST). This phenomenon changes the physical appearance of the polymer, helical and linear form, at the biorecognition interface. The chip surface was double functionalized with the PNIPAAm and a model ligand, biotin, and the antigen-antibody affinity reaction was observed and traced by surface plasmon resonance (SPR) spectroscopy. The amount of anti-biotin antibody binding on the chip surface was controlled specifically by the structural transformation of PNIPAAm by the temperature variation. By using two reaction channels on a single SPR sensor chip, the difference of the bound antibody concentration in the consequence of the structural transformation was found to be 3.73 × 10-13 mol cm-2, supporting the possibility of site-selective protein immobilization/patterning for multiplexed analysis.
AB - We describe the modulation of biointerface by an external stimulus with a smart polymer-modified electrode. Poly(N-isopropylacrylamide) (PNIPAAm) shows a rapid reversible hydrophilic/hydrophobic transition of its conformation in response to the temperature variation across its lower critical solution temperature (LCST). This phenomenon changes the physical appearance of the polymer, helical and linear form, at the biorecognition interface. The chip surface was double functionalized with the PNIPAAm and a model ligand, biotin, and the antigen-antibody affinity reaction was observed and traced by surface plasmon resonance (SPR) spectroscopy. The amount of anti-biotin antibody binding on the chip surface was controlled specifically by the structural transformation of PNIPAAm by the temperature variation. By using two reaction channels on a single SPR sensor chip, the difference of the bound antibody concentration in the consequence of the structural transformation was found to be 3.73 × 10-13 mol cm-2, supporting the possibility of site-selective protein immobilization/patterning for multiplexed analysis.
KW - Biospecific recognition
KW - Heat-sensitive polymer
KW - Poly(N-isopropylacrylamide)
KW - SPR
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U2 - 10.1016/j.colsurfa.2007.04.139
DO - 10.1016/j.colsurfa.2007.04.139
M3 - Article
AN - SCOPUS:37349052043
SN - 0927-7757
VL - 313-314
SP - 504
EP - 508
JO - Colloids and Surfaces A: Physicochemical and Engineering Aspects
JF - Colloids and Surfaces A: Physicochemical and Engineering Aspects
ER -