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On/off-switchable LSPR nano-immunoassay for troponin-T
Linköpings universitet, Institutionen för fysik, kemi och biologi, Biosensorer och bioelektronik. Linköpings universitet, Tekniska fakulteten. UCS, Institute Adv Mat, Teknikringen 4A,Mjardevi Science Pk, SE-58330 Linkoping, Sweden.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Biosensorer och bioelektronik. Linköpings universitet, Tekniska fakulteten. UCS, Institute Adv Mat, Teknikringen 4A,Mjardevi Science Pk, SE-58330 Linkoping, Sweden.
Royal Institute Technology, Sweden.
University of Kiel, Germany.
Vise andre og tillknytning
2017 (engelsk)Inngår i: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, artikkel-id 44027Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Regeneration of immunosensors is a longstanding challenge. We have developed a re-usable troponin-T (TnT) immunoassay based on localised surface plasmon resonance (LSPR) at gold nanorods (GNR). Thermosensitive poly(N-isopropylacrylamide) (PNIPAAM) was functionalised with anti-TnT to control the affinity interaction with TnT. The LSPR was extremely sensitive to the dielectric constant of the surrounding medium as modulated by antigen binding after 20 min incubation at 37 degrees C. Computational modelling incorporating molecular docking, molecular dynamics and free energy calculations was used to elucidate the interactions between the various subsystems namely, IgG-antibody (c. f., anti-TnT), PNIPAAM and/or TnT. This study demonstrates a remarkable temperature dependent immuno-interaction due to changes in the PNIPAAM secondary structures, i.e., globular and coil, at above or below the lower critical solution temperature (LCST). A series of concentrations of TnT were measured by correlating the lambda(LSPR) shift with relative changes in extinction intensity at the distinct plasmonic maximum (i. e., 832 nm). The magnitude of the red shift in lambda(LSPR) was nearly linear with increasing concentration of TnT, over the range 7.6 x 10(-15) to 9.1 x 10(-4) g/mL. The LSPR based nano-immunoassay could be simply regenerated by switching the polymer conformation and creating a gradient of microenvironments between the two states with a modest change in temperature.

sted, utgiver, år, opplag, sider
NATURE PUBLISHING GROUP , 2017. Vol. 7, artikkel-id 44027
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-136859DOI: 10.1038/srep44027ISI: 000398592100001PubMedID: 28382946OAI: oai:DiVA.org:liu-136859DiVA, id: diva2:1092123
Merknad

Funding Agencies|Institute of Advanced Materials (IAAM) [00554/2013-16]; Swedish Institute (SI) [00037/2014]; Linkoping Initiative in Life Science Technologies (LIST); Vinoba Bhave Research Institute [VBRI 2016/Res-01]; Linkoping University; Swedish Research Council [VR-2016-06014]

Tilgjengelig fra: 2017-04-30 Laget: 2017-04-30 Sist oppdatert: 2018-03-19

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