AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
PDF (8.3 MB)
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Research Article | Open Access

Enhancement of the Chemiluminescence Response of Enzymatic Reactions by Plasmonic Surfaces for Biosensing Applications

Biebele AbelBabatunde OdukoyaMuzaffer MohammedKadir Aslan( )
Morgan State University, Department of Chemistry, 1700 East Cold Spring Lane, Baltimore, MD 21251 USA
Show Author Information

Abstract

We report the enhancement of chemiluminescence response of horseradish peroxidase (HRP) in bioassays by plasmonic surfaces, which are comprised of (i) silver island films (SIFs) and (ii) metal thin films (silver, gold, copper, and nickel, 1 nm thick) deposited onto glass slides. A model bioassay, based on the interactions of avidin-modified HRP with a monolayer of biotinylated poly(ethylene-glycol)-amine, was employed to evaluate the ability of plasmonic surfaces to enhance chemiluminescence response of HRP. Chemiluminescence response of HRP in model bioassays were increased up to ~3.7-fold as compared to the control samples (i.e. glass slides without plasmonic nanoparticles), where the largest enhancement of the chemiluminescence response was observed on SIFs with high loading. These findings allowed us to demonstrate the use of SIFs (high loading) for the detection of a biologically relevant target protein (glial fibrillary acidic protein or GFAP), where the chemiluminescence response of the standard bioassay for GFAP was enhanced up to ~50% as compared to bioassay on glass slides.

References

[1]

Q.Y. Zhang, H. Chen, Z. Lin, et al., Comparison of chemiluminescence enzyme immunoassay based on magnetic microparticles with traditional colorimetric ELISA for the detection of serum α-fetoprotein, Journal of Pharmaceutical Analysis, 2012, 2: 130-135.

[2]

T.B. Xin, S.X. Liang, X. Wang, et al., Determination of estradiol in human serum using magnetic particles-based chemiluminescence immunoassay, Analytica chimica acta, 2008, 627: 277-284.

[3]

J.A. Ocaña-González, M. Ramos-Payán, R. Fernández-Torres, et al., Application of chemiluminescence in the analysis of wastewaters-A review. Talanta, 2014, 122: 214-222.

[4]

W. Liu, J. Kou, H. Xing, et al., Paper-based chromatographic chemiluminescence chip for the detection of dichlorvos in vegetables, Biosens Bioelectron, 2014, 52: 76-81.

[5]

M. Sorouraddin, M. Iranifam, A. Imani-Nabiyyi, Determination of penicillin V potassium in pharmaceuticals and spiked human urine by chemiluminescence, Central European Journal of Chemistry, 2009, 7: 143-147.

[6]

M. Iranifam, M. Fathinia, T. Sadeghi Rad, et al., A novel selenium nanoparticles-enhanced chemiluminescence system for determination of dinitrobutylphenol, Talanta, 2013, 107: 263-269.

[7]

J. Chen, D. Chen, T. Yuan, et al., Microfluidic PCR chips, Nano Biomed Eng, 2011, 3: 203-210.

[8]

A.N. Diaz, J.G. Garcia, J. Lovillo, Enhancer effect of fluorescein on the luminol–H2O2–horseradish peroxidase chemiluminescence: energy transfer process, J Biolumin Chemilumin, 1997, 12: 199-205.

[9]

G. Thorpe, L.J. Kricka, S. Moseley, et al., Phenols as enhancers of the chemiluminescent horseradish peroxidase-luminol-hydrogen peroxide reaction: application in luminescence-monitored enzyme immunoassays, Clinical chemistry, 1985, 31: 1335-1341.

[10]

H. Kawasaki, K. Sato, J. Ogawa, et al., Determination of inorganic phosphate by flow injection method with immobilized enzymes and chemiluminescence detection, Anal Biochem, 1989, 182: 366-370.

[11]

C.A. Swindlehurst, T.A. Nieman, Flow-injection determination of sugars with immobilized enzyme reactions and chemiluminescence detection, Analytica Chimica Acta, 1988, 205: 195-205.

[12]

D. Tian, H. Zhang, Y. Chai, et al., Synthesis of N-(aminobutyl)-N-(ethylisoluminol) functionalized gold nanomaterials for chemiluminescent bio-probe, Chem Commun (Camb), 2011, 47: 4959-4961.

[13]

N. Li, W. Wang, D. Tian, et al., pH-dependent catalytic properties of Pd-Ag nanoparticles in luminol chemiluminescence, Chem Commun (Camb), 2010, 46: 1520-1522.

[14]

C.F. Duan, H. Cui, Time-tunable autocatalytic lucigenin chemiluminescence initiated by platinum nanoparticles and ethanol, Chem Commun (Camb), 2009, 18: 2574-2576.

[15]

K. Aslan, C. D. Geddes, Metal - enhanced chemiluminescence: advanced chemiluminescence concepts for the 21st century, Chem Soc Rev, 2009, 38: 2556-2564.

[16]

B. Abel, K. Aslan, Immobilization of enzymes to silver island films for enhanced enzymatic activity, J Colloid Interface Sci, 2014, 415: 133-142.

[17]

B. Abel, K. Aslan, Plasmon-Enhanced Enzymatic Reactions 2: Optimization of Enzyme Activity by Surface Modification of Silver Island Films with Biotin-Poly (Ethylene-glycol)-Amine, Nano Biomed Eng, 2012, 4: 23-28.

[18]

B. Abel, T. C. Clement, K. Aslan; Enhancement of enzymatic colorimetric response by silver island films on high throughput screening microplates. J Immunol Methods 2014, 411: 43-49.

[19]

B. Abel, A. Akinsule, C. Andrews, et al., PlasmonEnhanced Enzymatic Reactions: A Study of NanoparticleEnzyme Distance-and Nanoparticle Loading-Dependent Enzymatic Activity, Nano biomedicine and engineering, 2011, 3: 184.

[20]

B. Abel, K. Aslan, Surface modification of plasmonic nanostructured materials with thiolated oligonucleotides in 10 seconds using selective microwave heating, Ann Phys, 2012, 524: 741-750.

[21]
A. Carré, W. Birch, V. Lacarrière, Glass Substrates Modified With Organosilanes For DNA Immobilization, in Silanes and Other Coupling Agents, Volume 4. 2007.
[22]

J.P. O’callaghan, Quantification of glial fibrillary acidic protein: comparison of slot-immunobinding assays with a novel sandwich ELISA, Neurotoxicol Teratol, 1991, 13: 275-281.

[23]

M.H. Chowdhury, K. Aslan, S.N. Malyn, et al., Metalenhanced chemiluminescence, Journal of Fluorescence, 2006, 16: 295-299.

[24]

M.H. Chowdhury, S.N. Malyn, K. Aslan, et al., First Observation of Surface Plasmon-Coupled Chemiluminescence (SPCC), Chem Phys Lett, 2007, 435: 114-118.

[25]

K. Aslan, C. D. Geddes, Metal - enhanced chemiluminescence: advanced chemiluminescence concepts for the 21st century, Chemical Society Reviews, 2009, 38: 2556-2564.

[26]

A.M. Alabanza, M. Mohammed, K. Aslan, Crystallization of l-alanine in the presence of additives on a circular PMMA platform designed for metal-assisted and microwave-accelerated evaporative crystallization, CrystEngComm, 2012, 14: 8424-8431.

[27]

B. Abel, T.S. Kabir, B. Odukoya, et al., Enhancement of Colorimetric Response of Enzymatic Reactions by Thermally Evaporated Plasmonic Thin Films: Application to Glial Fibrillary Acidic Protein, Anal Methods, 2015, 7: 1175-1185.

[28]

K. Rechendorff, M.B. Hovgaard, M. Foss, et al., Enhancement of protein adsorption induced by surface roughness, Langmuir, 2006, 22: 10885-10888.

[29]

K. Aslan, M. Weisenberg, E. Hortle, et al., Fixedangle observation of surface plasmon coupled chemiluminescence from palladium thin films, Applied Physics Letters, 2009, 95: 123117-123113.

[30]

K. Aslan, M.J.R. Previte, Y. Zhang, et al., Surface plasmon coupled fluorescence in the ultraviolet and visible spectral regions using zinc thin films, Analytical chemistry, 2008, 80: 7304-7312.

[31]

K. Aslan, C.D. Geddes, Surface plasmon coupled chemiluminescence from zinc substrates: Directional chemiluminescence, Applied Physics Letters, 2009, 94: 073104.

[32]

K. Aslan, C.D. Geddes, Metal-Enhanced Fluorescence: Progress Towards a Unified Plasmon-Fluorophore Description, Metal-Enhanced Fluorescence, 2010, 1-23.

[33]

Y. Wada, C. Yanagihara, Y. Nishimura, et al., Familial adult-onset Alexander disease with a novel mutation (D78N) in the glial fibrillary acidic protein gene with unusual bilateral basal ganglia involvement, J Neurol Sci, 2013, 331: 161-164.

[34]
A. Messing, Astrocytes and Alexander disease the first, but not last, primary astrocyte disease, in Physiology and pathophysiology of neuroglia, in Henry Stewart Talks: London. p. 1 streaming video file. 2011.
[35]

P.L. Jany, T.L. Hagemann, A. Messing, GFAP expression as an indicator of disease severity in mouse models of Alexander disease, ASN Neuro, 2013, 5: e00109.

Nano Biomedicine and Engineering
Pages 92-101
Cite this article:
Abel B, Odukoya B, Mohammed M, et al. Enhancement of the Chemiluminescence Response of Enzymatic Reactions by Plasmonic Surfaces for Biosensing Applications. Nano Biomedicine and Engineering, 2015, 7(3): 92-101. https://doi.org/10.5101/nbe.v7i3.p92-101

360

Views

9

Downloads

7

Crossref

7

Scopus

Altmetrics

Received: 01 August 2015
Accepted: 10 September 2015
Published: 15 September 2015
© 2015 Suphanchai Punthawanunt, Biebele Abel, Babatunde Odukoya, Muzaffer Mohammed and Kadir Aslan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Return