Selective antigen-antibody recognition on SPR sensor based on the heat-sensitive conformational change of poly(N-isopropylacrylamide)

Seung Yeon Song, Hyoung Gil Choi, Jung Woo Hong, Byung Woo Kim, Sang Jun Sim, Hyun C. Yoon

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)504-508
Number of pages5
JournalColloids and Surfaces A: Physicochemical and Engineering Aspects
Volume313-314
DOIs
Publication statusPublished - 2008 Feb 1
Externally publishedYes

    Fingerprint

Keywords

  • Biospecific recognition
  • Heat-sensitive polymer
  • Poly(N-isopropylacrylamide)
  • SPR

ASJC Scopus subject areas

  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry

Cite this