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Indirect Nanoplasmonic Sensing Platform for Monitoring Temperature-Dependent Protein Adsorption Full article

Journal Analytical Chemistry
ISSN: 0003-2700 , E-ISSN: 1520-6882
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 Jackman Joshua A. 1 , Ferhan Abdul Rahim 1 , Yoon Bo Kyeong 1 , Park Jae Hyeon 1 , Zhdanov Vladimir P. 1,3 , Cho Nam-Joon 1,2
Affiliations
1 School of Materials Science and Engineering and Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, 637553, Singapore
2 School of Chemical and Biomedical Engineering, Nanyang Technological University, 62 Nanyang Drive, 637459, Singapore
3 Boreskov Institute of Catalysis, Russian Academy of Sciences, Novosibirsk 630090, Russia

Funding (3)

1 Federal Agency for Scientific Organizations 0303-2016-0001
2 National Research Foundation of Singapore NRF-CRP10-2012-07
3 National Research Foundation of Singapore NRF2015NRF-POC0001-019

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 ANCAN PMID OpenAlex
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
Citing:
DB Citing
Web of science 35
Scopus 36
Elibrary 34
OpenAlex 40
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