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Journal articles on the topic 'Phosphopeptide enrichment'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Mullis, B. Todd, Sunil Hwang, L. Andrew Lee, et al. "Automating Complex, Multistep Processes on a Single Robotic Platform to Generate Reproducible Phosphoproteomic Data." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 3 (2019): 277–86. http://dx.doi.org/10.1177/2472555219878152.

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Mass spectrometry-based phosphoproteomics holds promise for advancing drug treatment and disease diagnosis; however, its clinical translation has thus far been limited. This is in part due to an unstandardized and segmented sample preparation process that involves cell lysis, protein digestion, peptide desalting, and phosphopeptide enrichment. Automating this entire sample preparation process will be key in facilitating standardization and clinical translation of phosphoproteomics. While peptide desalting and phosphopeptide enrichment steps have been individually automated, integrating these t

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2

Maccarrone, Giuseppina, Nikolaus Kolb, Larysa Teplytska, et al. "Phosphopeptide enrichment by IEF." ELECTROPHORESIS 27, no. 22 (2006): 4585–95. http://dx.doi.org/10.1002/elps.200600145.

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3

Ding, Fengjuan, Yameng Zhao, Haiyan Liu, and Weibing Zhang. "Core–shell magnetic microporous covalent organic framework with functionalized Ti(iv) for selective enrichment of phosphopeptides." Analyst 145, no. 12 (2020): 4341–51. http://dx.doi.org/10.1039/d0an00038h.

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We fabricated a core-shell magnetic Ti<sup>4+</sup>-functionalized covalent organic framework composite to selectively capture phosphopeptides in biosamples. This method is applicable to achieve rapid, selective and efficient phosphopeptide analysis.

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4

Ondrej, Martin, Pavel Rehulka, Helena Rehulkova, Rudolf Kupcik, and Ales Tichy. "Fractionation of Enriched Phosphopeptides Using pH/Acetonitrile-Gradient-Reversed-Phase Microcolumn Separation in Combination with LC–MS/MS Analysis." International Journal of Molecular Sciences 21, no. 11 (2020): 3971. http://dx.doi.org/10.3390/ijms21113971.

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Mass spectrometry (MS) is a powerful and sensitive method often used for the identification of phosphoproteins. However, in phosphoproteomics, there is an identified need to compensate for the low abundance, insufficient ionization, and suppression effects of non-phosphorylated peptides. These may hamper the subsequent liquid chromatography–mass spectrometry/mass spectrometry (LC–MS/MS) analysis, resulting in incomplete phosphoproteome characterization, even when using high-resolution instruments. To overcome these drawbacks, we present here an effective microgradient chromatographic technique

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5

Hou, Junjie, Zhensheng Xie, Peng Xue, et al. "Enhanced MALDI-TOF MS Analysis of Phosphopeptides Using an Optimized DHAP/DAHC Matrix." Journal of Biomedicine and Biotechnology 2010 (2010): 1–12. http://dx.doi.org/10.1155/2010/759690.

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Selecting an appropriate matrix solution is one of the most effective means of increasing the ionization efficiency of phosphopeptides in matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). In this study, we systematically assessed matrix combinations of 2, 6-dihydroxyacetophenone (DHAP) and diammonium hydrogen citrate (DAHC), and demonstrated that the low ratio DHAP/DAHC matrix was more effective in enhancing the ionization of phosphopeptides. Low femtomole level of phosphopeptides from the tryptic digests ofα-casein andβ-casein was readily detected by

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6

Palmisano, Giuseppe, Benjamin L. Parker, Kasper Engholm-Keller, et al. "A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development." Molecular & Cellular Proteomics 11, no. 11 (2012): 1191–202. http://dx.doi.org/10.1074/mcp.m112.017509.

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We describe a method that combines an optimized titanium dioxide protocol and hydrophilic interaction liquid chromatography to simultaneously enrich, identify and quantify phosphopeptides and formerly N-linked sialylated glycopeptides to monitor changes associated with cell signaling during mouse brain development. We initially applied the method to enriched membrane fractions from HeLa cells, which allowed the identification of 4468 unique phosphopeptides and 1809 formerly N-linked sialylated glycopeptides. We subsequently combined the method with isobaric tagging for relative quantification

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7

Gokmen-Polar, Yesim, Jason D. True, Edyta Vieth, Guihong D. Qi, Amber L. Mosley, and Sunil S. Badve. "Phosphopeptide mapping of DLC1 in ER+ breast cancer reveals AMOTL2, a key hippo pathway component, as an important target." Journal of Clinical Oncology 35, no. 15_suppl (2017): 11592. http://dx.doi.org/10.1200/jco.2017.35.15_suppl.11592.

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11592 Background: Metastases suppressor genes are believed to control tumor progression and metastases. Deleted in Liver Cancer 1 (DLC1) acts as a gatekeeper for tumor and metastasis suppression. Low expression of DLC1 correlates with poor prognosis in patients with ER+ breast cancer. It is essential to understand the impact of DLC1 and its functional network in preventing tumor and metastasis suppression. Methods: T47D cells with stable DLC1-Full-Length (DLC1-FL) were generated using mammalian expression cloning vector, pcDNA3.1+/C-(K)-DYK, and CloneEZ™ technology. Growth rate of control and

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8

Sandison, Mairi E., K. Tveen Jensen, F. Gesellchen, J. M. Cooper, and A. R. Pitt. "Magnetite-doped polydimethylsiloxane (PDMS) for phosphopeptide enrichment." Analyst 139, no. 19 (2014): 4974–81. http://dx.doi.org/10.1039/c4an00750f.

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9

Leitner, Alexander. "Phosphopeptide enrichment using metal oxide affinity chromatography." TrAC Trends in Analytical Chemistry 29, no. 2 (2010): 177–85. http://dx.doi.org/10.1016/j.trac.2009.08.007.

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10

Beltran, Luisa, and Pedro R. Cutillas. "Advances in phosphopeptide enrichment techniques for phosphoproteomics." Amino Acids 43, no. 3 (2012): 1009–24. http://dx.doi.org/10.1007/s00726-012-1288-9.

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11

Li, Liping, Shuai Chen, Linnan Xu, et al. "Template-free synthesis of uniform mesoporous SnO2 nanospheres for efficient phosphopeptide enrichment." J. Mater. Chem. B 2, no. 9 (2014): 1121–24. http://dx.doi.org/10.1039/c3tb21617a.

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12

Yan, Yinghua, Yujie Lu, Mengying Chen, and Hongze Liang. "A novel IMAC platform – adenosine coupled functional magnetic microspheres for phosphoproteome research." Analytical Methods 10, no. 10 (2018): 1190–95. http://dx.doi.org/10.1039/c7ay02931d.

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13

Li, Xiao-Shui, Bi-Feng Yuan, and Yu-Qi Feng. "Recent advances in phosphopeptide enrichment: Strategies and techniques." TrAC Trends in Analytical Chemistry 78 (April 2016): 70–83. http://dx.doi.org/10.1016/j.trac.2015.11.001.

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14

Krenkova, Jana, and Frantisek Foret. "Nanoparticle-modified monolithic pipette tips for phosphopeptide enrichment." Analytical and Bioanalytical Chemistry 405, no. 7 (2012): 2175–83. http://dx.doi.org/10.1007/s00216-012-6358-z.

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15

Warthaka, Mangalika, Paulina Karwowska-Desaulniers, and Mary Kay H. Pflum. "Phosphopeptide Modification and Enrichment by Oxidation–Reduction Condensation." ACS Chemical Biology 1, no. 11 (2006): 697–701. http://dx.doi.org/10.1021/cb6003564.

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16

Han, Guanghui, Mingliang Ye, and Hanfa Zou. "Development of phosphopeptide enrichment techniques for phosphoproteome analysis." Analyst 133, no. 9 (2008): 1128. http://dx.doi.org/10.1039/b806775a.

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17

Hung, Chien-Wen, Dieter Kübler, and Wolf D. Lehmann. "pI-based phosphopeptide enrichment combined with nanoESI-MS." ELECTROPHORESIS 28, no. 12 (2007): 2044–52. http://dx.doi.org/10.1002/elps.200600678.

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18

Zhang, Xumin, Juanying Ye, Ole N. Jensen, and Peter Roepstorff. "Highly Efficient Phosphopeptide Enrichment by Calcium Phosphate Precipitation Combined with Subsequent IMAC Enrichment." Molecular & Cellular Proteomics 6, no. 11 (2007): 2032–42. http://dx.doi.org/10.1074/mcp.m700278-mcp200.

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19

Hong, Yayun, Chenlu Pu, Hongli Zhao, Qianying Sheng, Qiliang Zhan, and Minbo Lan. "Yolk–shell magnetic mesoporous TiO2 microspheres with flowerlike NiO nanosheets for highly selective enrichment of phosphopeptides." Nanoscale 9, no. 43 (2017): 16764–72. http://dx.doi.org/10.1039/c7nr05330d.

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20

Yi, Linhua, Yinghua Yan, Keqi Tang, and Chuan-Fan Ding. "Facile preparation of polymer-grafted ZIF-8-modified magnetic nanospheres for effective identification and capture of phosphorylated and glycosylated peptides." Analytical Methods 12, no. 38 (2020): 4657–64. http://dx.doi.org/10.1039/d0ay01412e.

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21

Ahmed, Adnan, Vijay J. Raja, Paola Cavaliere, and Noah Dephoure. "Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate." Journal of Proteome Research 18, no. 3 (2018): 1411–17. http://dx.doi.org/10.1021/acs.jproteome.8b00883.

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22

SUI, S., J. WANG, Z. LU, et al. "Phosphopeptide enrichment strategy based on strong cation exchange chromatography." Chinese Journal of Chromatography 26, no. 2 (2008): 195–99. http://dx.doi.org/10.1016/s1872-2059(08)60012-7.

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23

Yu, Ying-Qing, Jennifer Fournier, Martin Gilar, and John C. Gebler. "Phosphopeptide enrichment using microscale titanium dioxide solid phase extraction." Journal of Separation Science 32, no. 8 (2009): 1189–99. http://dx.doi.org/10.1002/jssc.200800652.

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24

Krenkova, Jana, Jaroslava Moravkova, Jan Buk, and Frantisek Foret. "Phosphopeptide enrichment with inorganic nanofibers prepared by forcespinning technology." Journal of Chromatography A 1427 (January 2016): 8–15. http://dx.doi.org/10.1016/j.chroma.2015.12.022.

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25

Yue, Guihua Eileen, Michael G. Roper, Catherine Balchunas, et al. "Protein digestion and phosphopeptide enrichment on a glass microchip." Analytica Chimica Acta 564, no. 1 (2006): 116–22. http://dx.doi.org/10.1016/j.aca.2005.11.003.

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26

Yan, Shuang, Bin Luo, Jia He, Fang Lan, and Yao Wu. "Phytic acid functionalized magnetic bimetallic metal–organic frameworks for phosphopeptide enrichment." Journal of Materials Chemistry B 9, no. 7 (2021): 1811–20. http://dx.doi.org/10.1039/d0tb02517h.

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Novel bimetallic metal–organic framework nanocomposites were fabricated by a facile yet efficient method. The as-prepared nanomaterial exhibited high sensitivity and high selectivity toward phosphopeptides and good reusability of five cycles for enriching phosphopeptides.

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27

Tóth, Gábor, Fanni Bugyi, Simon Sugár, et al. "Selective TiO2 Phosphopeptide Enrichment of Complex Samples in the Nanogram Range." Separations 7, no. 4 (2020): 74. http://dx.doi.org/10.3390/separations7040074.

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Phosphopeptide enrichment is a commonly used sample preparation step for investigating phosphorylation. TiO2-based enrichment has been demonstrated to have excellent performance both for large amounts of complex and for small amounts of simple samples. However, it has not yet been studied for complex samples in the nanogram range. Our objective was to develop a methodology applicable for complex samples in the low nanogram range, useful for mass spectrometry analysis of tissue microarrays. The selectivity and performance of two stationary phases (TiO2 nanoparticle-coated monolithic column and

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28

Kume, Akinori, Akina Sasayama, Tetsuo Kaneko, Junichi Kurisaki та Munehiro Oda. "A simple competitive enzyme-linked immunosorbent assay for the specific detection of the multiphosphorylated 1–25 β-casein fragment". Journal of Dairy Research 80, № 3 (2013): 326–33. http://dx.doi.org/10.1017/s0022029913000162.

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A specific and simple competitive enzyme-linked immunosorbent assay (ELISA) was developed to determine bovine β-casein phosphopeptides (β-CPP) in casein phosphopeptides (CPP) or CPP complexes such as casein phosphopeptide amorphous calcium phosphate complexes added into dairy products. The method combines sample pretreatment designed for CPP enrichment and anti-β-CPP(f(1–25)) monoclonal antibody 1A5 (mAb 1A5). The mAb 1A5 bound specifically to the tryptic phosphopeptides from β-casein but not from αs1- or αs2-casein. Reactivity was also influenced by the extent of the phosphorylated form of se

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29

Tape, Christopher J., Jonathan D. Worboys, John Sinclair, et al. "Reproducible Automated Phosphopeptide Enrichment Using Magnetic TiO2 and Ti-IMAC." Analytical Chemistry 86, no. 20 (2014): 10296–302. http://dx.doi.org/10.1021/ac5025842.

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30

Kupcik, Rudolf, Jan M. Macak, Helena Rehulkova, et al. "Amorphous TiO2Nanotubes as a Platform for Highly Selective Phosphopeptide Enrichment." ACS Omega 4, no. 7 (2019): 12156–66. http://dx.doi.org/10.1021/acsomega.9b00571.

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31

Wang, Wei-Han, and Merlin L. Bruening. "Phosphopeptide enrichment on functionalized polymer microspots for MALDI-MS analysis." Analyst 134, no. 3 (2009): 512–18. http://dx.doi.org/10.1039/b815598d.

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32

Li, Qing-run, Zhi-bin Ning, Jia-shu Tang, Song Nie, and Rong Zeng. "Effect of Peptide-to-TiO2Beads Ratio on Phosphopeptide Enrichment Selectivity." Journal of Proteome Research 8, no. 11 (2009): 5375–81. http://dx.doi.org/10.1021/pr900659n.

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33

Zhao, Yanyan, Xiuling Li, Jingyu Yan, Zhimou Guo, and Xinmiao Liang. "Phosphopeptide enrichment and fractionation by using Click OEG-CD matrix." Analytical Methods 4, no. 5 (2012): 1244. http://dx.doi.org/10.1039/c2ay05915k.

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34

Batalha, Iris L., Houjiang Zhou, Kathryn Lilley, Christopher R. Lowe, and Ana C. A. Roque. "Mimicking nature: Phosphopeptide enrichment using combinatorial libraries of affinity ligands." Journal of Chromatography A 1457 (July 2016): 76–87. http://dx.doi.org/10.1016/j.chroma.2016.06.032.

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35

Leitner, Alexander, Martin Sturm, Jan-Henrik Smått, et al. "Optimizing the performance of tin dioxide microspheres for phosphopeptide enrichment." Analytica Chimica Acta 638, no. 1 (2009): 51–57. http://dx.doi.org/10.1016/j.aca.2009.01.063.

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36

Dunn, Jamie D., Elizabeth A. Igrisan, Amanda M. Palumbo, Gavin E. Reid, and Merlin L. Bruening. "Phosphopeptide Enrichment Using MALDI Plates Modified with High-Capacity Polymer Brushes." Analytical Chemistry 80, no. 15 (2008): 5727–35. http://dx.doi.org/10.1021/ac702472j.

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37

Mirza, Munazza Raza, Matthias Rainer, Yüksel Güzel, Iqbal M. Choudhary, and Günther K. Bonn. "A novel strategy for phosphopeptide enrichment using lanthanide phosphate co-precipitation." Analytical and Bioanalytical Chemistry 404, no. 3 (2012): 853–62. http://dx.doi.org/10.1007/s00216-012-6215-0.

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38

Tsougeni, Katerina, Panagiotis Zerefos, Angeliki Tserepi, Antonia Vlahou, Spiros D. Garbis, and Evangelos Gogolides. "TiO2–ZrO2 affinity chromatography polymeric microchip for phosphopeptide enrichment and separation." Lab on a Chip 11, no. 18 (2011): 3113. http://dx.doi.org/10.1039/c1lc20133f.

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39

BAI, Yu, LinNan XU, and HuWei LIU. "Amino-functionalized monolithic tips for rapid phosphopeptide enrichment with tunable selectivity." SCIENTIA SINICA Vitae 48, no. 2 (2017): 207–14. http://dx.doi.org/10.1360/n052017-00171.

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40

Murillo, Jimmy Rodriguez, Magdalena Kuras, Melinda Rezeli, Tasso Milliotis, Lazaro Betancourt, and Gyorgy Marko-Varga. "Automated phosphopeptide enrichment from minute quantities of frozen malignant melanoma tissue." PLOS ONE 13, no. 12 (2018): e0208562. http://dx.doi.org/10.1371/journal.pone.0208562.

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41

Negroni, Luc, Stephane Claverol, Jean Rosenbaum, Eric Chevet, Marc Bonneu, and Jean-Marie Schmitter. "Comparison of IMAC and MOAC for phosphopeptide enrichment by column chromatography." Journal of Chromatography B 891-892 (April 2012): 109–12. http://dx.doi.org/10.1016/j.jchromb.2012.02.028.

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42

Chen, Jing, Sudhirkumar Shinde, Prabal Subedi, et al. "Validation of molecularly imprinted polymers for side chain selective phosphopeptide enrichment." Journal of Chromatography A 1471 (November 2016): 45–50. http://dx.doi.org/10.1016/j.chroma.2016.10.018.

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43

Wu, Ting, Jiani Shi, Chuanjing Zhang, Lingfan Zhang, and Yiping Du. "Highly specific phosphopeptide enrichment by titanium(IV) cross-linked chitosan composite." Journal of Chromatography B 1008 (January 2016): 234–39. http://dx.doi.org/10.1016/j.jchromb.2015.11.051.

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44

Zhang, Haiyang, Xiaowei Li, Shujuan Ma, Junjie Ou, Yinmao Wei, and Mingliang Ye. "One-step preparation of phosphate-rich carbonaceous spheres via a hydrothermal approach for phosphopeptide analysis." Green Chemistry 21, no. 8 (2019): 2052–60. http://dx.doi.org/10.1039/c8gc03706j.

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45

Zhu, Gang-Tian, Xiao-Mei He, Sheng He, Xi Chen, Shu-Kui Zhu, and Yu-Qi Feng. "Synthesis of Polyethylenimine Functionalized Mesoporous Silica for In-Pipet-Tip Phosphopeptide Enrichment." ACS Applied Materials & Interfaces 8, no. 47 (2016): 32182–88. http://dx.doi.org/10.1021/acsami.6b10948.

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46

Tan, Yu-Jing, Dexin Sui, Wei-Han Wang, Min-Hao Kuo, Gavin E. Reid, and Merlin L. Bruening. "Phosphopeptide Enrichment with TiO2-Modified Membranes and Investigation of Tau Protein Phosphorylation." Analytical Chemistry 85, no. 12 (2013): 5699–706. http://dx.doi.org/10.1021/ac400198n.

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47

Murillo, Jimmy Rodriguez, Magdalena Kuras, Melinda Rezeli, Tasso Miliotis, Lazaro Betancourt, and Gyorgy Marko-Varga. "Correction: Automated phosphopeptide enrichment from minute quantities of frozen malignant melanoma tissue." PLOS ONE 13, no. 12 (2018): e0210234. http://dx.doi.org/10.1371/journal.pone.0210234.

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48

Wan, Huihui, Jingyu Yan, Long Yu, et al. "Zirconia layer coated mesoporous silica microspheres used for highly specific phosphopeptide enrichment." Talanta 82, no. 5 (2010): 1701–7. http://dx.doi.org/10.1016/j.talanta.2010.07.050.

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49

Li, Wangwang, Qiliang Deng, Guozhen Fang, Yang Chen, Jie Zhan, and Shuo Wang. "Facile synthesis of Fe3O4@TiO2–ZrO2 and its application in phosphopeptide enrichment." Journal of Materials Chemistry B 1, no. 14 (2013): 1947. http://dx.doi.org/10.1039/c3tb20127a.

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50

Abelin, Jennifer G., Paisley D. Trantham, Sarah A. Penny, et al. "Complementary IMAC enrichment methods for HLA-associated phosphopeptide identification by mass spectrometry." Nature Protocols 10, no. 9 (2015): 1308–18. http://dx.doi.org/10.1038/nprot.2015.086.

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