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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378271%3A_____%2F21%3A00552381" target="_blank" >RIV/68378271:_____/21:00552381 - isvavai.cz</a>

Výsledek na webu

<a href="http://hdl.handle.net/11104/0327527" target="_blank" >http://hdl.handle.net/11104/0327527</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acsami.1c05950" target="_blank" >10.1021/acsami.1c05950</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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).

Název v anglickém jazyce

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

Popis výsledku anglicky

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).

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10609 - Biochemical research methods

Projekt

<a href="/cs/project/EF18_053%2F0016627" target="_blank" >EF18_053/0016627: Mobilita výzkumných, technických a administrativních pracovníků FZU</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ACS Applied Materials and Interfaces

ISSN

1944-8244

e-ISSN

1944-8252

Svazek periodika

13

Číslo periodika v rámci svazku

23

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

27645-27655

Kód UT WoS článku

000664289800096

EID výsledku v databázi Scopus

2-s2.0-85108386869