Indirect Nanoplasmonic Sensing Platform for Monitoring Temperature-Dependent Protein Adsorption Full article
Journal |
Analytical Chemistry
ISSN: 0003-2700 , E-ISSN: 1520-6882 |
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Output data | Year: 2017, Volume: 89, Number: 23, Pages: 12976-12983 Pages count : 8 DOI: 10.1021/acs.analchem.7b03921 | ||||||
Tags | BOVINE SERUM-ALBUMIN; SURFACE-PLASMON RESONANCE; INDUCED CONFORMATIONAL-CHANGES; SOLID-SURFACES; REFRACTIVE-INDEX; GOLD NANOPARTICLES; ALPHA-LACTALBUMIN; LIGHT-SCATTERING; STEEL SURFACES; IONIC-STRENGTH | ||||||
Authors |
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Affiliations |
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Funding (3)
1 | National Research Foundation of Singapore | NRF-CRP10-2012-07 |
2 | National Research Foundation of Singapore | NRF2015NRF-POC0001-019 |
3 | Federal Agency for Scientific Organizations | 0303-2016-0001 |
Abstract:
The development of highly surface-sensitive measurement approaches to monitor protein adsorption across different temperatures would advance understanding of how thermally activated processes contribute to the denaturation of adsorbed proteins. Herein, we established an indirect nanoplasmonic sensing approach to monitor the temperature-dependent adsorption and denaturation of bovine serum albumin (BSA) protein onto a silica-coated array of plasmonic gold nanodisks. A theoretical model was developed to explain how the denaturation of an individual, adsorbed protein molecule influences the localized surface plasmon resonance (LSPR) measurement response and provided an analytical framework to estimate the effect of temperature-dependent protein denaturation on the corresponding adsorption kinetics. The sensing performance of this measurement platform was also characterized across the tested range of temperatures. With increasing temperature (up to 50 °C), it was observed that adsorbed proteins undergo greater denaturation. Circular dichroism spectroscopy and dynamic light scattering experiments verified that individual BSA monomers in bulk solution had increasingly lower conformational stability at higher temperatures within this range, which correlated with the extent of denaturation in the adsorbed state. At higher temperatures, distinct kinetic profiles arising from multilayer/aggregate formation on the sensor surface were also detected. Taken together, our findings identify that the high surface sensitivity and temperature stability of LSPR sensors make them broadly useful analytical tools for monitoring thermally activated biomacromolecular interaction processes.
Cite:
Jackman J.A.
, Ferhan A.R.
, Yoon B.K.
, Park J.H.
, Zhdanov V.P.
, Cho N-J.
Indirect Nanoplasmonic Sensing Platform for Monitoring Temperature-Dependent Protein Adsorption
Analytical Chemistry. 2017. V.89. N23. P.12976-12983. DOI: 10.1021/acs.analchem.7b03921 WOS Scopus РИНЦ
Indirect Nanoplasmonic Sensing Platform for Monitoring Temperature-Dependent Protein Adsorption
Analytical Chemistry. 2017. V.89. N23. P.12976-12983. DOI: 10.1021/acs.analchem.7b03921 WOS Scopus РИНЦ
Files:
Full text from publisher
Dates:
Submitted: | Sep 25, 2017 |
Published online: | Nov 7, 2017 |
Published print: | Dec 5, 2017 |
Identifiers:
Web of science | WOS:000417549600052 |
Scopus | 2-s2.0-85037526886 |
Elibrary | 35515468 |
Chemical Abstracts | 2017:1768724 |
Chemical Abstracts (print) | 167:584074 |
PMID | 29111680 |
OpenAlex | W2767822840 |