Lab-on-a-chip dielectrophoretic manipulation of beta-2 microglobulin for toxin removal in an artificial kidney

Background: This paper presents a fundamental study of protein manipulation under the influence of dielectrophoretic (DEP) force for a lab-on-a-chip platform. Objective: Protein manipulation is dependent on the polarisation factor of protein when exposed to an electric field. Therefore the objective...

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Bibliographic Details
Published in:Micro and Nanosystems
Main Author: Samad M.I.A.; Kayani A.A.; Zoolfakar A.S.; Hamzah A.A.; Majlis B.Y.; Buyong M.R.
Format: Article
Language:English
Published: Bentham Science Publishers B.V. 2019
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85066738238&doi=10.2174%2f1876402911666181218145459&partnerID=40&md5=8fc3e7d7017e5ac2144b059062830e0a
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Summary:Background: This paper presents a fundamental study of protein manipulation under the influence of dielectrophoretic (DEP) force for a lab-on-a-chip platform. Objective: Protein manipulation is dependent on the polarisation factor of protein when exposed to an electric field. Therefore the objective of this work is a microfluidic device and measurement system are used to characterise the human beta-2 microglobulin (β2M) protein via lateral attractive forces and vertical repulsive forces by means of DEP responses. Method: The manipulation of the β2M protein was conducted using a microfluidic platform with a tapered DEP microelectrode and the protein concentration was quantified based on a biochemical interaction using an Enzyme-Linked Immunosolvent Assay (ELISA). The protein distribution has been analysed based on the β2M concentration for each microfluidic outlet. Results: At 300 kHz, the protein experienced a negative DEP (nDEP) with of 83.3% protein distribution on the middle microchannel. In contrast, the protein experienced a positive DEP (pDEP) at 1.2 MHz with of 78.7% of protein on the left and right sides of the microchannel. Conclusion: This is concept proved that the tapered DEP microelectrode is capable of manipulating a β2M via particle polarisation, hence making it suitable to be utilised for purifying proteins in biomedical application. © 2019 Bentham Science Publishers.
ISSN:18764029
DOI:10.2174/1876402911666181218145459