Responsive Hydrogel Binding Matrix for Dual Signal Amplification in Fluorescence Affinity Biosensors and Peptide Microarrays
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
PubMed
34081862
DOI
10.1021/acsami.1c05950
Knihovny.cz E-zdroje
- Klíčová slova
- biomarkers, click chemistry, microarrays, pNIPAAm, peptide, plasmon-enhanced fluorescence, serotesting, thermoresponsive hydrogel,
- MeSH
- akrylové pryskyřice chemie MeSH
- biosenzitivní techniky metody MeSH
- fluorescence MeSH
- hydrogely chemie metabolismus MeSH
- imunoglobulin G analýza imunologie MeSH
- infekce virem Epsteina-Barrové diagnóza imunologie metabolismus virologie MeSH
- lidé MeSH
- peptidové fragmenty imunologie metabolismus MeSH
- polymery chemie MeSH
- virus Epsteinův-Barrové - jaderné antigeny imunologie MeSH
- virus Epsteinův-Barrové imunologie izolace a purifikace MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- akrylové pryskyřice MeSH
- hydrogely MeSH
- imunoglobulin G MeSH
- peptidové fragmenty MeSH
- poly-N-isopropylacrylamide MeSH Prohlížeč
- polymery MeSH
- virus Epsteinův-Barrové - jaderné antigeny MeSH
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). The detection is performed in diluted human plasma or with isolated human IgG by using a set of peptide ligands mapping the epitope of the EBV nuclear antigen. Alkyne-terminated peptides were covalently coupled to the pNIPAAm-based HG carrying azide moieties. Importantly, using such low-molecular-weight ligands allowed preserving the thermoresponsive properties of the pNIPAAm-based architecture, which was not possible for amine coupling of regular antibodies that have a higher molecular weight.
FZU Institute of Physics Czech Academy of Sciences Na Slovance 2 Prague 182 21 Czech Republic
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