An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor

In recent decades, there was a surge of interest in Surface Plasmon Resonance (SPR) biosensor based bimolecular interaction analysis. The unique characteristics of this technique made it possible to measure real time unlabelled bimolecular interactions with great sensitivity. However, the major chal...

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Main Authors: Honari, Parisa, Allaudin, Zeenathul Nazariah, Mohd Lila, Mohd Azmi, Mustafa, Nor Hidayah
Format: Article
Language:English
Published: Academic Journals 2011
Online Access:http://psasir.upm.edu.my/id/eprint/25318/
http://psasir.upm.edu.my/id/eprint/25318/1/25318.pdf
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author Honari, Parisa
Allaudin, Zeenathul Nazariah
Mohd Lila, Mohd Azmi
Mustafa, Nor Hidayah
author_facet Honari, Parisa
Allaudin, Zeenathul Nazariah
Mohd Lila, Mohd Azmi
Mustafa, Nor Hidayah
author_sort Honari, Parisa
building UPM Institutional Repository
collection Online Access
description In recent decades, there was a surge of interest in Surface Plasmon Resonance (SPR) biosensor based bimolecular interaction analysis. The unique characteristics of this technique made it possible to measure real time unlabelled bimolecular interactions with great sensitivity. However, the major challenge in SPR is providing the ability to re-use the surface of the chip. The main goal of this study was to address the problem faced in establishing an ideal regeneration condition and removing noncovalently bound analyt without disturbing ligand. Considering four different types of proteins including virus, hormone, cells and antibody, a comprehensive regeneration protocol for proteinprotein interaction was developed and compared with common regeneration methods. The presented protocol screened five multi-ingredient stock solutions that represented the five most common chemical properties such as acidic, basic, ionic, chelating and non-polar water soluble solvent solutions employed as regeneration agents. Upon three cycles of screening, it was found out that enveloped virus-antibody complexes could be effectively regenerated via a combination of acidic and chelating solution whilst non-enveloped viruses needed a basic solution for successful regeneration. Both insulin-antibody and cell-enveloped virus complexes could be detached efficiently using acidic solutions. Regenerations using non-polar water soluble solvents presented a harsh reaction, whilst ionic solutions were too mild. Thus, incomplete regeneration occurred. In summary, this study will serve as a platform of reference for multiple regenerations for a cluster of protein-protein complexes.
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spelling upm-253182017-11-10T08:36:55Z http://psasir.upm.edu.my/id/eprint/25318/ An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor Honari, Parisa Allaudin, Zeenathul Nazariah Mohd Lila, Mohd Azmi Mustafa, Nor Hidayah In recent decades, there was a surge of interest in Surface Plasmon Resonance (SPR) biosensor based bimolecular interaction analysis. The unique characteristics of this technique made it possible to measure real time unlabelled bimolecular interactions with great sensitivity. However, the major challenge in SPR is providing the ability to re-use the surface of the chip. The main goal of this study was to address the problem faced in establishing an ideal regeneration condition and removing noncovalently bound analyt without disturbing ligand. Considering four different types of proteins including virus, hormone, cells and antibody, a comprehensive regeneration protocol for proteinprotein interaction was developed and compared with common regeneration methods. The presented protocol screened five multi-ingredient stock solutions that represented the five most common chemical properties such as acidic, basic, ionic, chelating and non-polar water soluble solvent solutions employed as regeneration agents. Upon three cycles of screening, it was found out that enveloped virus-antibody complexes could be effectively regenerated via a combination of acidic and chelating solution whilst non-enveloped viruses needed a basic solution for successful regeneration. Both insulin-antibody and cell-enveloped virus complexes could be detached efficiently using acidic solutions. Regenerations using non-polar water soluble solvents presented a harsh reaction, whilst ionic solutions were too mild. Thus, incomplete regeneration occurred. In summary, this study will serve as a platform of reference for multiple regenerations for a cluster of protein-protein complexes. Academic Journals 2011-11-09 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/25318/1/25318.pdf Honari, Parisa and Allaudin, Zeenathul Nazariah and Mohd Lila, Mohd Azmi and Mustafa, Nor Hidayah (2011) An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor. African Journal of Biotechnology, 10 (70). art. no. 56E2E7D30173. pp. 15795-15800. ISSN 1684–5315 http://www.academicjournals.org/journal/AJB/article-abstract/56E2E7D30173 10.5897/AJB11.1486
spellingShingle Honari, Parisa
Allaudin, Zeenathul Nazariah
Mohd Lila, Mohd Azmi
Mustafa, Nor Hidayah
An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor
title An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor
title_full An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor
title_fullStr An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor
title_full_unstemmed An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor
title_short An approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor
title_sort approach towards optimal usage of immobilized sensor chips in surface plasmon resonance based biosensor
url http://psasir.upm.edu.my/id/eprint/25318/
http://psasir.upm.edu.my/id/eprint/25318/
http://psasir.upm.edu.my/id/eprint/25318/
http://psasir.upm.edu.my/id/eprint/25318/1/25318.pdf