Responsive hydrogel binding matrix for dual signal amplification in fluorescence affinity biosensors and peptide microarrays

0552381 - FZÚ 2022 RIV US eng J - Journal Article
Hageneder, S. - Jungbluth, V. - Soldo, R. - Petri, C. - Pertiller, M. - Kreivi, M. - Weinhaeusel, A. - Jonas, U. - Dostálek, Jakub
Responsive hydrogel binding matrix for dual signal amplification in fluorescence affinity biosensors and peptide microarrays.
ACS Applied Materials and Interfaces. Roč. 13, č. 23 (2021), s. 27645-27655. ISSN 1944-8244. E-ISSN 1944-8252
R&D Projects: GA MŠMT(CZ) EF18_053/0016627
Grant - others:OP VVV - Mobility FZU 2(XE) CZ.02.2.69/0.0/0.0/18_053/0016627
Institutional support: RVO:68378271
Keywords : thermoresponsive hydrogel * pNIPAAm * plasmon-enhanced fluorescence * microarrays * click chemistry * peptide * serotesting * biomarkers
OECD category: Biochemical research methods
Impact factor: 10.383, year: 2021
Method of publishing: Open access

A combined approach to signal enhancement in fluorescence affinity biosensors and assays is reported. It is based on the compaction of specifically captured target molecules at the sensor surface followed by optical probing with a tightly confined surface plasmon (SP) field. This concept is utilized by using a thermoresponsive hydrogel(HG) binding matrix that is prepared from a terpolymer derived from poly(N-isopropylacrylamide) (pNIPAAm) and attached to a metallic sensor surface. Epi-illumination fluorescence and SP-enhanced total internal reflection fluorescence readouts of affinity binding events are performed to spatially interrogate the fluorescent signal in the direction parallel and perpendicular to the sensor surface. The pNIPAAm-based HG binding matrix is arranged in arrays of sensing spots and employed for the specific detection of human IgG antibodies against the Epstein−Barr virus (EBV).
Permanent Link: http://hdl.handle.net/11104/0327527