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

journal contribution
posted on 2024-11-02, 21:59 authored by Nur Nasir, Revathy Deivasigamani, M. F. Wee, Azrul Hamzah, Mohd Zaid, Muhammad Rahim, Aminuddin Bin Ahmad Kayani, Abdullah Abdulhameed, Muhamad Buyong
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.

History

Journal

Micromachines

Volume

13

Number

1308

Issue

8

Start page

1

End page

21

Total pages

21

Publisher

MDPI AG

Place published

Switzerland

Language

English

Copyright

© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)

Former Identifier

2006119228

Esploro creation date

2023-03-31

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