Paper Titles
Effects of Al2O3 Additive on Manganese Phosphate Conversion Coating of Carbon Steel
p.81
Influence of Cold Spraying Process on the Bonding Strength of Ni-Al2O3-Zn Coating
p.91
Absorption Rate Evaluation of Fabric-Foam-Fabric Plied Material
p.97
Preparation and Experimental Study of Graphite Material for Water Lubricated Thrust Bearing of Nuclear Main Pump
p.102
Preparation of Nano-TiO2 Modified Temperature-Responsive Chromatographic Materials for Enrichment of Phosphopeptides
p.109
One-Pot Preparation of Carbon Immobilized Nano-Metal Catalysts from Biomass
p.119
Adsorption of Heavy Metals Using γ-PGA Produced by Bacillus pumilus
p.124
The Preparation and Performance of the Cement-Based Concrete 3D Printing Materials
p.131
Properties of Low Water/Cement Ratio and High Compressive Strength Pervious Concrete
p.136

Preparation of Nano-TiO2 Modified Temperature-Responsive Chromatographic Materials for Enrichment of Phosphopeptides

Article Preview

Abstract:

Chromatographic stationary phases with specific capturing phosphoproteins is widely used in biological sample pretreatment. However, when captured protein is released, it is required to change the pH of the mobile phase or to use an eluent. Usually, the mobile phase or eluent are salt solutions with high concentration and extreme pH or toxic organic reagents. In this situation, these reagents will destroy the activity and structure of phosphorylated proteins. In addition, the mobile phase after switching the column takes longer time to restore the balance, reducing the experimental efficiency. In order to solve the these problems, we introduce temperature-reponsive materials into the chromatographic stationary phase to achieve the capture and release of phosphorylated proteins by changing the temperature only, in which we use water as the mobile phase. This approach overcomes the drawbacks of traditional methods, and makes the separation process safe and simple. Based on the surface initiated Reversible Addition Fragmentation Chain Transfer Polymerization (SI-RAFT) method, silica@pNIPAAm-nanoTiO2, a kind of Metal Oxide Affinity Chromatography, was synthesized by the rapid introduction of functional groups. The synthesis of silica@pNIPAAm-nanoTiO2 was confirmed by infrared and X-ray photoelectron spectroscopy. The grafting rate and the lowest critical temperature were measured by TG and DSC. The results showed that the material had qualified temperature-sensitive properties. The grafting conformation and mobile phase pH of the material were optimized before testing the properties and found that when the material grafting ratio was 10% -15%, the graft density was 30%, and the mobile phase pH was 6, it had the best separate effect. Finally, the material successfully achieved the capture and release of adenosine triphosphate and casein phosphopeptides.

You might also be interested in these eBooks
Material Engineering and Manufacturing View Preview

Info:

Periodical:

Materials Science Forum (Volume 932)

Pages:

109-118

DOI:

https://doi.org/10.4028/www.scientific.net/MSF.932.109

Citation:

Cite this paper

Online since:

September 2018

Authors:

Xinzhu Pang, Jin Sheng Feng, Di Wang, Bo Li, Xiao Qiong Li, Yu Lin Deng, Rong Ji Dai

Keywords:

Metal Oxide Affinity Chromatography, Nano-TiO2, Phosphorylated Protein, Temperature-Responsive

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

© 2018 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

References

[1] J. Ptacek, G. Devgan, G. Michaud, H. Zhu, X. Zhu, J. Fasolo, H. Guo, G. Jona, A.Bretkreutz, R. Sopko, R.R. McCartney, M.C. Schmidt, N. Rachidi, S.J. Lee, A.S. Mah, L. Meng, M.J.R. Stark, D. Stern, C.D. Virgilio, M. Tyers, B. Andrews, M.Gerstein, B. Schweitzer, P.F. Predki, M. Snyder, Global analysis of proteinphosphorylation in yeast, Nature 438 (2005).

DOI: 10.1038/nature04187

Google Scholar

[2] S. Morandell, T. Stasyk, K. Grosstessner-Hain, E. Roitinger, K. Mechtler, G.K. Bonn, L.A. Huber, Phosphoproteomics strategies for the functional analysis of signal transduction, Proteomics 6 (2006) 4047–4056.

DOI: 10.1002/pmic.200600058

Google Scholar

[3] K. Schmelzle, F.M. White, Phosphoproteomic approaches to elucidate cellular signaling networks, Curr. Opin. Biotechnol. 17 (2006) 406–414.

DOI: 10.1016/j.copbio.2006.06.004

Google Scholar

[4] T.E. Thingholm, O.N. Jensen, M.R. Larsen, Analytical strategies for phosphoproteomics, Proteomics 9 (2009) 1451–1468.

DOI: 10.1002/pmic.200800454

Google Scholar

[5] Ficarro, S. B., et al. Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nature Biotechnology20 (2002) 301-5.

Google Scholar

[6] J.D. Dunn, G.E. Reid, M.L. Bruening, Techniques for phosphopeptide enrichment prior to analysis by mass spectrometry, Mass Spectrom. Rev. 29 (2010) 29–54.

DOI: 10.1002/mas.20219

Google Scholar

[7] Nühse, Thomas S., et al. Large-scale Analysis of in Vivo Phosphorylated Membrane Proteins by Immobilized Metal Ion Affinity Chromatography and Mass Spectrometry. Molecular & Cellular Proteomics 2 (2003) 1234-1243.

DOI: 10.1074/mcp.t300006-mcp200

Google Scholar

[8] Yang D. S., Ding X. Y., Min H. P., et al. Design and synthesis of an immobilized metal affinity chromatography and metal oxide affinity chromatography hybrid material for improved phosphopeptide enrichment. Journal of Chromatography A, 7 (2017).

DOI: 10.1016/j.chroma.2017.05.025

Google Scholar

[9] Alpert, A.J.,O. Hudecz, and K. Mechtler. Anion-exchange chromatography of phosphopeptides: weak anion exchange versus strong anion exchange and anion-exchange chromatography versus electrostatic repulsion-hydrophilic interaction chromatography. Analytical Chemistry. 87 (2015).

DOI: 10.1021/ac504420c

Google Scholar

[10] C.L. Nilsson, Advances in quantitative phosphoproteomics, Anal. Chem. 84 (2012) 735–746.

Google Scholar

[11] Nonglaton, G, et al. New approach to oligonucleotide microarrays using zirconium phosphonate-modified surfaces.Journal of the American Chemical Society. 126 (2004) 1497-502.

DOI: 10.1021/ja039072r

Google Scholar

[12] Zhou, H., et al. Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis. Journal of Proteome Research. 7 (2008) 3957.

DOI: 10.1021/pr800223m

Google Scholar

[13] Wijeratne A B, Wijesundera D N, Paulose M, et al. Phosphopeptide Separation Using Radially Aligned Titania Nanotubes on Titanium Wire [J]. ACS Applied Materials & Interfaces, 2015, 7(21): 11155-11164.

DOI: 10.1021/acsami.5b00799

Google Scholar

[14] Zhang Y, Li J, Niu F, et al. Comparison of a novel TiO2/diatomite composite and pure TiO2 for the purification of phosvitin phosphopeptides [J]. Journal of Chromatography B, 2014, 960: 52-58.

DOI: 10.1016/j.jchromb.2014.03.038

Google Scholar

[15] Huang X, Wang J, Liu C, et al. A novel rGR-TiO2-ZrO2 composite nanosheet for capturing phosphopeptides from biosamples [J]. Journal of Materials Chemistry B, 2015, 3(12): 2505-2515.

DOI: 10.1039/c4tb01899k

Google Scholar

[16] Li X S, Chen X, Sun H, et al. Perovskite for the highly selective enrichment of phosphopeptides [J]. Journal of Chromatography A, 2015, 1376: 143-148.

DOI: 10.1016/j.chroma.2014.12.036

Google Scholar

[17] Larsen M R, Thingholm T E, Jensen O N, et al. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns [J]. Molecular & Cellular Proteomics, 2005, 4(7): 873-886.

DOI: 10.1074/mcp.t500007-mcp200

Google Scholar

[18] Deng Z, Dong M, Yan W, et al. A biphasic affinity chromatographic approach for deep tyrosine phosphoproteome analysis [J]. Analytical Chemistry, 2017, 89(4): 2405-2410.

DOI: 10.1021/acs.analchem.6b04288

Google Scholar

[19] Q. Zhang, N Tang, J, Brock, Enrichment and analysis of nonenzymatically glycated peptides: Boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry, Journal of Proteome Research 6 (2007) 2323-2330.

DOI: 10.1021/pr070112q.s001

Google Scholar

[20] E.S. Gil, S.M. Hudson, Stimuli-reponsive polymers and their bioconjugates, Progress in Polymer Science. 29 (2004) 1173-1222.

DOI: 10.1016/j.progpolymsci.2004.08.003

Google Scholar

[21] H. Kanazawa, T. Okano, Temperature-responsive chromatography for the separation of biomolecules, Journal of Chromatography A. 1218 (2011) 8738-8744.

DOI: 10.1016/j.chroma.2011.04.015

Google Scholar

[22] Gil, Eun Seok, and S. M. Hudson. Stimuli-reponsive polymers and their bioconjugates., Progress in Polymer Science. 29 (2004) 1173-1222.

DOI: 10.1016/j.progpolymsci.2004.08.003

Google Scholar

[23] R.J. Dai, C. Lei, Z. Liu, Preparation and characterization of temperature-responsive chromatographic column containing poly(N-isopropylacrylamide) and poly([2-(methacryloyloxy)- ethyl]trimetylammonium chloride), Journal of Applied Polymer Science. 121 (2011).

DOI: 10.1002/app.33830

Google Scholar

[24] Y.Y. Shen, L.L. Dong, Y.L. Liang, Z.J. Liu, R.J. Dai, W.W. Meng, Y.L. Deng, Effect of the grafting ratio of poly(N-isopropylacrylamide) on thermally responsive polymer brush surfaces, Journal of Separation Science. 40 (2016) 254-531.

DOI: 10.1002/jssc.201600890

Google Scholar