Verification of the Universal Versatility of a Quantitative Protein Measurement Technique Using a Metal Mesh Device

Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry
Seiji KambaYoshiko Miura

Abstract

When proteins are attached to microstructures such as a metal mesh device, changes in their optical properties occur. These changes have been characterized based on actual measurements in the infrared region of the spectrum. We have previously theoretically and experimentally demonstrated the optical changes associated with streptavidin. Here, we investigate three types of proteins: avidin, BSA, and lysozyme. The three proteins were adsorbed onto three types of metal mesh devices having different resonant frequencies, and the corresponding spectra were measured in the infrared region. The change in the frequency of the dip point in the spectrum was extracted to quantitatively determine the quantity of protein; these results were correlated with the quantitative measurements obtained by electrophoresis. By examining three types of different proteins, it was verified that a variety of proteins can be measured based on the optical characteristics of metal mesh devices.

References

Feb 15, 2001·Physical Review Letters·L Martín-MorenoT W Ebbesen
Jul 25, 2003·Analytical and Bioanalytical Chemistry·Jirí Homola
Jul 13, 2004·Science·J B PendryF J Garcia-Vidal
Apr 22, 2006·Optics Letters·F MiyamaruE Kato
Aug 1, 1967·Applied Optics·R D Rawcliffe, C M Randall
Jul 3, 2013·Langmuir : the ACS Journal of Surfaces and Colloids·Hirokazu SetoYoshiko Miura
Mar 15, 2015·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Hirokazu SetoYoshiko Miura
Sep 12, 2017·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Seiji KambaYoshiko Miura

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Citations

Feb 5, 2019·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Hirokazu SetoHiroyuki Shinto

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