TY - JOUR
T1 - Orders-of-magnitude larger force demonstrated for dielectrophoresis of proteins enabling high-resolution separations based on new mechanisms
AU - Liu, Yameng
AU - Hayes, Mark A.
N1 - Funding Information:
Dmitry Matyushov is acknowledged for his insightful and valuable discussions, and Blanca Lapizco-Encinas is acknowledged for broad discussions about nonlinear electric field effects. This work was supported by the URI ASU Innovation Hub Collaborative Research Seed Grant and National Institutes of Health grant 5R03AI133397-02.
Publisher Copyright:
© 2020 American Chemical Society
PY - 2021/1/26
Y1 - 2021/1/26
N2 - Proteins are perhaps the most important yet frustratingly complicated and difficult class of compounds to analyze, manipulate, and use. One very attractive option to characterize and differentially concentrate proteins is dielectrophoresis, but according to accepted theory, the force on smaller particles the size of proteins is too low to overcome diffusive action. Here, three model proteins, immunoglobulin G, α-chymotrypsinogen A, and lysozyme, are shown to generate forces much larger than predicted by established theory are more consistent with new theoretical constructs, which include the dipole moment and interfacial polarizability. The forces exerted on the proteins are quantitatively measured against well-established electrophoretic and diffusive processes and differ for each. These forces are orders of magnitude larger than previously predicted and enable the selective isolation and concentration of proteins consistent with an extremely high-resolution separation and concentration system based on the higher-order electric properties. The separations occur over a small footprint, happen quickly, and can be made in series or parallel (and in any order) on simple devices.
AB - Proteins are perhaps the most important yet frustratingly complicated and difficult class of compounds to analyze, manipulate, and use. One very attractive option to characterize and differentially concentrate proteins is dielectrophoresis, but according to accepted theory, the force on smaller particles the size of proteins is too low to overcome diffusive action. Here, three model proteins, immunoglobulin G, α-chymotrypsinogen A, and lysozyme, are shown to generate forces much larger than predicted by established theory are more consistent with new theoretical constructs, which include the dipole moment and interfacial polarizability. The forces exerted on the proteins are quantitatively measured against well-established electrophoretic and diffusive processes and differ for each. These forces are orders of magnitude larger than previously predicted and enable the selective isolation and concentration of proteins consistent with an extremely high-resolution separation and concentration system based on the higher-order electric properties. The separations occur over a small footprint, happen quickly, and can be made in series or parallel (and in any order) on simple devices.
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U2 - 10.1021/acs.analchem.0c02763
DO - 10.1021/acs.analchem.0c02763
M3 - Article
AN - SCOPUS:85099099142
SN - 0003-2700
VL - 93
SP - 1352
EP - 1359
JO - Analytical Chemistry
JF - Analytical Chemistry
IS - 3
ER -