Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/87502
Full metadata record
DC FieldValueLanguage
dc.contributor.authorJackman, Joshua A.en
dc.contributor.authorSut, Tun Nawen
dc.contributor.authorCho, Nam-Joonen
dc.contributor.authorFerhan, Abdul Rahimen
dc.date.accessioned2018-07-31T04:37:39Zen
dc.date.accessioned2019-12-06T16:43:15Z-
dc.date.available2018-07-31T04:37:39Zen
dc.date.available2019-12-06T16:43:15Z-
dc.date.issued2018en
dc.identifier.citationFerhan, A. R., Jackman, J. A., Sut, T. N., & Cho, N.-J. (2018). Quantitative comparison of protein adsorption and conformational changes on dielectric-coated nanoplasmonic sensing arrays. Sensors, 18(4), 1283-.en
dc.identifier.issn1424-8220en
dc.identifier.urihttps://hdl.handle.net/10356/87502-
dc.identifier.urihttp://hdl.handle.net/10220/45406en
dc.description.abstractNanoplasmonic sensors are a popular, surface-sensitive measurement tool to investigate biomacromolecular interactions at solid-liquid interfaces, opening the door to a wide range of applications. In addition to high surface sensitivity, nanoplasmonic sensors have versatile surface chemistry options as plasmonic metal nanoparticles can be coated with thin dielectric layers. Within this scope, nanoplasmonic sensors have demonstrated promise for tracking protein adsorption and substrate-induced conformational changes on oxide film-coated arrays, although existing studies have been limited to single substrates. Herein, we investigated human serum albumin (HSA) adsorption onto silica- and titania-coated arrays of plasmonic gold nanodisks by localized surface plasmon resonance (LSPR) measurements and established an analytical framework to compare responses across multiple substrates with different sensitivities. While similar responses were recorded on the two substrates for HSA adsorption under physiologically-relevant ionic strength conditions, distinct substrate-specific behavior was observed at lower ionic strength conditions. With decreasing ionic strength, larger measurement responses occurred for HSA adsorption onto silica surfaces, whereas HSA adsorption onto titania surfaces occurred independently of ionic strength condition. Complementary quartz crystal microbalance-dissipation (QCM-D) measurements were also performed, and the trend in adsorption behavior was similar. Of note, the magnitudes of the ionic strength-dependent LSPR and QCM-D measurement responses varied, and are discussed with respect to the measurement principle and surface sensitivity of each technique. Taken together, our findings demonstrate how the high surface sensitivity of nanoplasmonic sensors can be applied to quantitatively characterize protein adsorption across multiple surfaces, and outline broadly-applicable measurement strategies for biointerfacial science applications.en
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en
dc.format.extent14 p.en
dc.language.isoenen
dc.relation.ispartofseriesSensorsen
dc.rights© 2018 by The Author(s). Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).en
dc.subjectNanoplasmonicsen
dc.subjectLocalized Surface Plasmon Resonanceen
dc.titleQuantitative comparison of protein adsorption and conformational changes on dielectric-coated nanoplasmonic sensing arraysen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen
dc.contributor.schoolSchool of Materials Science and Engineeringen
dc.contributor.researchCentre for Biomimetic Sensor Scienceen
dc.identifier.doihttp://dx.doi.org/10.3390/s18041283en
dc.description.versionPublished versionen
item.grantfulltextopen-
item.fulltextWith Fulltext-
Appears in Collections:MSE Journal Articles
SCBE Journal Articles

Google ScholarTM

Check

Altmetric

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.