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Protein Albumin Manipulation and Electrical Quantification of Molecular Dielectrophoresis Responses for Biomedical Applications

Journal

MICROMACHINES
Volume 13, Issue 8, Pages -

Publisher

MDPI
DOI: 10.3390/mi13081308

Keywords

dielectrophoresis; electrical quantification; protein; manipulation

Funding

  1. Malaysian Ministry of Higher Education [AKU254]
  2. Universiti Kebangsaan Malaysia (UKM [PRGS/1/2021/TK04/UKM/02/1]
  3. Australian Research Council [IH210100040]
  4. Australian Research Council [IH210100040] Funding Source: Australian Research Council

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This article reviews three methods of electrical quantification of DEP responses and discusses their correlation with DEP responses. The study found that capacitance measurement is a reliable method for identifying DEP responses. Furthermore, the possibility of manipulating proteins and electrically quantifying DEP responses without the usage of dye or fluorescent probes is discussed.
Research relating to dielectrophoresis (DEP) has been progressing rapidly through time as it is a strong and controllable technique for manipulation, separation, preconcentration, and partitioning of protein. Extensive studies have been carried out on protein DEP, especially on Bovine Serum Albumin (BSA). However, these studies involve the usage of dye and fluorescent probes to observe DEP responses as the physical properties of protein albumin molecular structure are translucent. The use of dye and the fluorescent probe could later affect the protein's physiology. In this article, we review three methods of electrical quantification of DEP responses: electrochemical impedance spectroscopy (EIS), cyclic voltammetry (CV) and capacitance measurement for protein BSA DEP manipulation. The correlation of these methods with DEP responses is further discussed. Based on the observations on capacitance measurement, it can be deduced that the electrical quantifying method is reliable for identifying DEP responses. Further, the possibility of manipulating the protein and electrically quantifying DEP responses while retaining the original physiology of the protein and without the usage of dye or fluorescent probe is discussed.

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