Indirect Nanoplasmonic Sensing Platform for Monitoring Temperature-Dependent Protein Adsorption | Sciact - CRIS-система Института катализа

Indirect Nanoplasmonic Sensing Platform for Monitoring Temperature-Dependent Protein Adsorption Научная публикация

Журнал

Analytical Chemistry
ISSN: 0003-2700 , E-ISSN: 1520-6882

Вых. Данные

Год: 2017, Том: 89, Номер: 23, Страницы: 12976-12983 Страниц : 8 DOI: 10.1021/acs.analchem.7b03921

Ключевые слова

BOVINE SERUM-ALBUMIN; SURFACE-PLASMON RESONANCE; INDUCED CONFORMATIONAL-CHANGES; SOLID-SURFACES; REFRACTIVE-INDEX; GOLD NANOPARTICLES; ALPHA-LACTALBUMIN; LIGHT-SCATTERING; STEEL SURFACES; IONIC-STRENGTH

Авторы

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

Организации

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

Информация о финансировании (3)

1	Федеральное агентство научных организаций России	0303-2016-0001
2	National Research Foundation of Singapore	NRF-CRP10-2012-07
3	National Research Foundation of Singapore	NRF2015NRF-POC0001-019

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.

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 CAPlusCA PMID OpenAlex

Полный текст от издателя

Поступила в редакцию:	25 сент. 2017 г.
Опубликована online:	7 нояб. 2017 г.
Опубликована в печати:	5 дек. 2017 г.

Web of science:	WOS:000417549600052
Scopus:	2-s2.0-85037526886
РИНЦ:	35515468
Chemical Abstracts:	2017:1768724
Chemical Abstracts (print):	167:584074
PMID (PubMed):	29111680
OpenAlex:	W2767822840

БД	Цитирований
Web of science	35
Scopus	35
РИНЦ	32
OpenAlex	39