CE-MS for Proteomics and Intact Protein Analysis.

Saraswathy N, Ramalingam P, Saraswathy N, Ramalingam P (2011) Mass spectrometry for proteomics. Concepts Tech Genomics Proteomics:171–183. https://doi.org/10.1533/9781908818058.171

Velghe S, Capiau S, Stove CP (2016) Opening the toolbox of alternative sampling strategies in clinical routine: a key-role for (LC-)MS/MS. TrAC Trends Anal Chem 84:61–73. https://doi.org/10.1016/J.TRAC.2016.01.030

doi: 10.1016/j.trac.2016.01.030

Shi Y, Xiang R, Horváth C, Wilkins JA (2004) The role of liquid chromatography in proteomics. J Chromatogr A 1053:27–36. https://doi.org/10.1016/J.CHROMA.2004.07.044

pubmed: 15543969 doi: 10.1016/S0021-9673(04)01204-X

Michalski A, Cox J, Mann M (2011) More than 100,000 detectable peptide species elute in single shotgun proteomics runs but the majority is inaccessible to data-dependent LC−MS/MS. J Proteome Res 10:1785–1793. https://doi.org/10.1021/pr101060v

pubmed: 21309581 doi: 10.1021/pr101060v

Schiavone NM, Sarver SA, Sun L et al (2015) High speed capillary zone electrophoresis–mass spectrometry via an electrokinetically pumped sheath flow interface for rapid analysis of amino acids and a protein digest. J Chromatogr B 991:53–58. https://doi.org/10.1016/J.JCHROMB.2015.04.001

doi: 10.1016/j.jchromb.2015.04.001

Neusüß C, Pelzing M, Macht M (2002) A robust approach for the analysis of peptides in the low femtomole range by capillary electrophoresis-tandem mass spectrometry. Electrophoresis 23:3149–3159. https://doi.org/10.1002/1522-2683(200209)23:18<3149::AID-ELPS3149>3.0.CO;2-8

pubmed: 12298087 doi: 10.1002/1522-2683(200209)23:18<3149::AID-ELPS3149>3.0.CO;2-8

Boley DA, Zhang Z, Dovichi NJ (2018) Multisegment injections improve peptide identification rates in capillary zone electrophoresis-based bottom-up proteomics. J Chromatogr A 1523:123–126. https://doi.org/10.1016/j.chroma.2017.07.022.Multisegment

doi: 10.1016/j.chroma.2017.07.022

Ramautar R, Heemskerk AAM, Hensbergen PJ et al (2012) CE-MS for proteomics: advances in interface development and application. J Proteomics 75:3814–3828. https://doi.org/10.1016/j.jprot.2012.04.050

pubmed: 22609513 doi: 10.1016/j.jprot.2012.04.050

Schmidt A, Karas M, Dülcks T (2003) Effect of different solution flow rates on analyte ion signals in nano-ESI MS, or: when does ESI turn into nano-ESI? J Am Soc Mass Spectrom 14:492–500. https://doi.org/10.1016/S1044-0305 (03)00128-4

pubmed: 12745218 doi: 10.1016/S1044-0305(03)00128-4

Wilm M, Mann M (1996) Analytical properties of the nanoelectrospray ion source. Anal Chem 68:1–8. https://doi.org/10.1021/ac9509519

pubmed: 8779426 doi: 10.1021/ac9509519 pmcid: 8779426

Klein J, Papadopoulos T, Mischak H, Mullen W (2014) Comparison of CE-MS/MS and LC-MS/MS sequencing demonstrates significant complementarity in natural peptide identification in human urine. Electrophoresis 35:1060–1064. https://doi.org/10.1002/elps.201300327

pubmed: 24254231 doi: 10.1002/elps.201300327

Iadarola P, Fumagalli M, Bardoni AM et al (2016) Recent applications of CE- and HPLC-MS in the analysis of human fluids. Electrophoresis 37:212–230. https://doi.org/10.1002/elps.201500272

pubmed: 26426542 doi: 10.1002/elps.201500272 pmcid: 26426542

Di Venere M, Viglio S, Sassera D et al (2017) Do the complementarities of electrokinetic and chromatographic procedures represent the “Swiss knife” in proteomic investigation? An overview of the literature in the past decade. Electrophoresis 38:1538–1550. https://doi.org/10.1002/elps.201600504

pubmed: 28130906 doi: 10.1002/elps.201600504 pmcid: 28130906

Jooß K, Scholz N, Meixner J, Neusüß C (2019) Heart-cut nano-LC-CZE-MS for the characterization of proteins on the intact level. Electrophoresis:1–5. https://doi.org/10.1002/elps.201800411

Breadmore MC (2009) Electrokinetic and hydrodynamic injection: making the right choice for capillary electrophoresis. Bioanalysis 1:889–894. https://doi.org/10.4155/bio.09.73

pubmed: 21083060 doi: 10.4155/bio.09.73 pmcid: 21083060

Larsson M, Lutz ESM (2000) Transient isotachophoresis for sensitivity enhancement in capillary electrophoresis- mass spectrometry for peptide analysis CE and CEC. Electrophoresis 21:2859–2865

pubmed: 11001295 doi: 10.1002/1522-2683(20000801)21:14<2859::AID-ELPS2859>3.0.CO;2-F pmcid: 11001295

Mala Z, Bocek P, Gebauer P (2013) Recent progress in analytical capillary isotachophoresis. Electrophoresis 34:19–28. https://doi.org/10.1002/elps.201200323

pubmed: 23161365 doi: 10.1002/elps.201200323 pmcid: 23161365

Osbourn DM, Weiss DJ, Lunte CE (2008) On-line preconcentration methods for capillary electrophoresis. Electrophoresis 21:2768–2779. https://doi.org/10.1002/1522-2683(20000801)21

doi: 10.1002/1522-2683(20000801)21:14<2768::AID-ELPS2768>3.0.CO;2-P

Gahoual R, Busnel JM, Beck A et al (2014) Full antibody primary structure and microvariant characterization in a single injection using transient isotachophoresis and sheathless capillary electrophoresis-tandem mass spectrometry. Anal Chem 86:9074–9081. https://doi.org/10.1021/ac502378e

pubmed: 25141158 doi: 10.1021/ac502378e pmcid: 25141158

Monton MRN, Imami K, Nakanishi M et al (2005) Dynamic pH junction technique for on-line preconcentration of peptides in capillary electrophoresis. J Chromatogr A 1079:266–273. https://doi.org/10.1016/j.chroma.2005.03.069

pubmed: 16038313 doi: 10.1016/j.chroma.2005.03.069 pmcid: 16038313

Aebersold R, Morrison HD (1990) Analysis of dilute peptide samples by capillary zone electrophoresis. J Chromatogr 516:79–88

pubmed: 2286630 doi: 10.1016/S0021-9673(01)90206-7 pmcid: 2286630

Nesbitt CA, Lo JT, Yeung KK (2005) Over 1000-fold protein preconcentration for microliter-volume samples at a pH junction using capillary electrophoresis. J Chromatogr A 1073:175–180. https://doi.org/10.1016/j.chroma.2004.09.081

pubmed: 15909520 doi: 10.1016/j.chroma.2004.09.081 pmcid: 15909520

Hasan N, Park SH, Oh E, Song EJ, Ban E, Yoo YS (2010) Sensitivity enhancement of CE and CE-MS for the analysis of peptides by a dynamic pH junction. J Sep Sci 33:3701–3709. https://doi.org/10.1002/jssc.201000020

pubmed: 21082675 doi: 10.1002/jssc.201000020 pmcid: 21082675

Lombard-Banek C, Reddy S, Moody SA, Nemes P (2016) Label-free quantification of proteins in single embryonic cells with neural fate in the cleavage-stage frog (Xenopus laevis) embryo using capillary electrophoresis electrospray ionization high-resolution mass spectrometry (CE-ESI-HRMS). Mol Cell Proteomics 15:2756–2768. https://doi.org/10.1074/mcp.M115.057760

pubmed: 27317400 pmcid: 4974349 doi: 10.1074/mcp.M115.057760

Monton MRN, Terabe S (2004) Field-enhanced sample injection for high-sensitivity analysis of peptides and proteins in capillary electrophoresis – mass spectrometry. J Chromatogr A 1032:203–211. https://doi.org/10.1016/j.chroma.2003.10.038

pubmed: 15065797 doi: 10.1016/j.chroma.2003.10.038 pmcid: 15065797

Pourhaghighi MR, Busnel J-M, Girault HH (2011) High-sensitive protein analysis by FESI-CE-MALDI-MS. Electrophoresis 32:1795–1803. https://doi.org/10.1002/elps.201100024

pubmed: 21710548 doi: 10.1002/elps.201100024 pmcid: 21710548

Zhu G, Sun L, Yan X, Dovichi NJ (2014) Bottom-up proteomics of Escherichia coli using dynamic pH junction preconcentration and capillary zone electrophoresis-electrospray ionization-tandem mass spectrometry. Anal Chem 86(13):6331–6336

pubmed: 24852005 pmcid: 4082393 doi: 10.1021/ac5004486

Arnett SD, Lunte CE (2008) Investigation of the mechanism of pH-mediated stacking of anions for the analysis of physiological samples by capillary electrophoresis. Electrophoresis 24:1745–1752. https://doi.org/10.1002/elps.200305399.Investigation

doi: 10.1002/elps.200305399

Dong Y-M, Chien K, Chen J et al (2013) Site-specific separation and detection of phosphopeptide isomers with pH-mediated stacking capillary electrophoresis- electrospray ionization-tandem mass spectrometry. J Sep Sci 36:1582–1589. https://doi.org/10.1002/jssc.201300054

pubmed: 23494885 doi: 10.1002/jssc.201300054 pmcid: 23494885

Dawod M, Chung DS (2011) High-sensitivity capillary and microchip electrophoresis using electrokinetic supercharging. J Sep Sci 34:2790–2799. https://doi.org/10.1002/jssc.201100384

pubmed: 21793208 doi: 10.1002/jssc.201100384

Xu Z, Ando T, Nishine T et al (2003) Electrokinetic supercharging preconcentration and microchip gel electrophoretic separation of sodium dodecyl sulfate-protein complexes. Electrophoresis 24:3821–3827. https://doi.org/10.1002/elps.200305625

pubmed: 14613211 doi: 10.1002/elps.200305625

Busnel J-M, Niels L, Girault HH (2008) Electrokinetic supercharging for highly efficient peptide preconcentration in capillary zone electrophoresis. Electrophoresis 29:1565–1572. https://doi.org/10.1002/elps.200700643

pubmed: 18384030 doi: 10.1002/elps.200700643

Nyssen L, Fillet M, Cavalier E, Servais A-C (2019) Highly sensitive and selective separation of intact parathyroid hormone and variants by sheathless CE-ESI-MS/MS. Electrophoresis:1–25. https://doi.org/10.1002/elps.201800507

Xu Z, Timerbaev AR, Hirokawa T (2009) High-sensitivity capillary and microchip electrophoresis using electrokinetic supercharging preconcentration insight into the stacking mechanism via computer modeling. J Chromatogr A 1216:660–670. https://doi.org/10.1016/j.chroma.2008.10.077

pubmed: 18996535 doi: 10.1016/j.chroma.2008.10.077

Sun L, Hebert AS, Yan X et al (2014) Over 10 000 peptide identifications from the HeLa proteome by using single-shot capillary zone electrophoresis combined with tandem mass spectrometry. Angew Chem Int Ed 53:13931–13933. https://doi.org/10.1002/anie.201409075

doi: 10.1002/anie.201409075

Zhang S, Raedschelders K, Santos M, Eyk JEV (2017) Profiling B-type natriuretic peptide cleavage peptidoforms in human plasma by capillary electrophoresis with electrospray ionization mass spectrometry. J Proteome Res 16:4515–4522. https://doi.org/10.1021/acs.jproteome.7b00482

pubmed: 28861997 doi: 10.1021/acs.jproteome.7b00482 pmcid: 28861997

Tempels FWA, Underberg WJM, Somsen GW, de Jong GJ (2007) On-line coupling of SPE and CE-MS for peptide analysis. Electrophoresis 28:1319–1326. https://doi.org/10.1002/elps.200600403

pubmed: 17351891 doi: 10.1002/elps.200600403 pmcid: 17351891

Pero-Gascon R, Pont L, Benavente F et al (2016) Analysis of serum transthyretin by on-line immunoaffinity solid-phase extraction capillary electrophoresis mass spectrometry using magnetic beads. Electrophoresis 37:1220–1231. https://doi.org/10.1002/elps.201500495

pubmed: 26842820 doi: 10.1002/elps.201500495 pmcid: 26842820

Xia S, Yuan H, Liang Z et al (2015) Particulate capillary precolumns with double-end polymer monolithic frits for on-line peptide trapping and preconcentration. Chin Chem Lett 26:1068–1072. https://doi.org/10.1016/j.cclet.2015.05.042

doi: 10.1016/j.cclet.2015.05.042

Morales-Cid G, Diez-Masa JC, Frutos MD (2013) On-line immunoaffinity capillary electrophoresis based on magnetic beads for the determination of alpha-1 acid glycoprotein isoforms profile to facilitate its use as biomarker. Anal Chim Acta 773:89–96. https://doi.org/10.1016/j.aca.2013.02.037

pubmed: 23561911 doi: 10.1016/j.aca.2013.02.037

Ortiz-Villanueva E, Benavente F, Giménez E et al (2014) Preparation and evaluation of open tubular C18-silica monolithic microcartridges for preconcentration of peptides by on-line solid phase extraction capillary electrophoresis. Anal Chim Acta 846:51–59. https://doi.org/10.1016/j.aca.2014.06.046

pubmed: 25220141 doi: 10.1016/j.aca.2014.06.046 pmcid: 25220141

Benavente F, Vescina MC, Hernández E et al (2007) Lowering the concentration limits of detection by on-line solid-phase extraction-capillary electrophoresis-electrospray mass spectrometry. J Chromatogr A 1140:205–212. https://doi.org/10.1016/j.chroma.2006.11.092

pubmed: 17174962 doi: 10.1016/j.chroma.2006.11.092 pmcid: 17174962

Zhang Z, Sun L, Zhu G et al (2015) Integrated strong cation-exchange hybrid monolith coupled with capillary zone electrophoresis and simultaneous dynamic pH junction for large-volume proteomic analysis by mass spectrometry. Talanta 138:117–122. https://doi.org/10.1016/j.talanta.2015.01.040

pubmed: 25863379 pmcid: 4394190 doi: 10.1016/j.talanta.2015.01.040

Chen Y, Wang K, Yang H et al (2012) Synthesis of sulfo/vinyl biphasic silica hybrid monolithic capillary column and its application to on-column preconcentration for capillary electrochromatography. J Chromatogr A 1233:91–99. https://doi.org/10.1016/j.chroma.2012.01.024

pubmed: 22410157 doi: 10.1016/j.chroma.2012.01.024 pmcid: 22410157

Benavente F, Hernández E, Guzman NA, Sanz-nebot V (2007) Determination of human erythropoietin by on-line immunoaffinity capillary electrophoresis: a preliminary report. Anal Bioanal Chem 387:2633–2639. https://doi.org/10.1007/s00216-007-1119-0

pubmed: 17265085 doi: 10.1007/s00216-007-1119-0 pmcid: 17265085

Medina-Casanellas S, Benavente F, Giménez E et al (2014) On-line immunoaffinity solid-phase extraction capillary electrophoresis mass spectrometry for the analysis of large biomolecules: a preliminary report. Electrophoresis 35:2130–2136. https://doi.org/10.1002/elps.201400119

pubmed: 24737614 doi: 10.1002/elps.201400293 pmcid: 24737614

Pont L, Benavente F, Barbosa J, Sanz-Nebot V (2017) On-line immunoaffinity solid-phase extraction capillary electrophoresis mass spectrometry using Fab’antibody fragments for the analysis of serum transthyretin. Talanta 170:224–232. https://doi.org/10.1016/j.talanta.2017.03.104

pubmed: 28501163 doi: 10.1016/j.talanta.2017.03.104 pmcid: 28501163

Peoples MC, Karnes HT (2008) Microfluidic capillary system for immunoaffinity separations of C-reactive protein in human serum and cerebrospinal fluid. Anal Chem 80:3853–3858

pubmed: 18399643 doi: 10.1021/ac800244n pmcid: 18399643

Amundsen LK, Siren H (2007) Immunoaffinity CE in clinical analysis of body fluids and tissues. Electrophoresis 28:99–113. https://doi.org/10.1002/elps.200500962

pubmed: 17149780 doi: 10.1002/elps.200500962 pmcid: 17149780

Breadmore MC, Sänger van de Griend CE (2016) In-capillary sample concentration in CE. LCGC N Am 32:174–186

Beckers JL, Bocek P (2003) The preparation of background electrolytes in capillary zone electrophoresis: golden rules and pitfalls. Electrophoresis 24:518–535

pubmed: 12569542 doi: 10.1002/elps.200390060

Pantuckova P, Gebauer P, Bocek P, Krivankova L (2009) Electrolyte systems for on-line CE – MS: detection requirements and separation possibilities. Electrophoresis 30:203–214. https://doi.org/10.1002/elps.200800262

pubmed: 19156660 doi: 10.1002/elps.200800262 pmcid: 19156660

Hruska V, Jaros M, Gas B (2006) Simul 5 – free dynamic simulator of electrophoresis. Electrophoresis 27:984–991. https://doi.org/10.1002/elps.200500756

pubmed: 16523464 doi: 10.1002/elps.200500756 pmcid: 16523464

Janini GM, Conrads TP, Wilkens KL et al (2003) A sheathless nanoflow electrospray interface for on-line capillary electrophoresis mass spectrometry. Anal Chem 75:1615–1619

pubmed: 12705593 doi: 10.1021/ac020661+ pmcid: 12705593

Catai JR, Torano JS, de Jong GJ, Somsen GW (2006) Efficient and highly reproducible capillary electrophoresis – mass spectrometry of peptides using Polybrene-poly (vinyl sulfonate)-coated capillaries. Electrophoresis 27:2091–2099. https://doi.org/10.1002/elps.200500915

pubmed: 16736451 doi: 10.1002/elps.200500915

Liu T, Li J, Zeng R et al (2001) Capillary electrophoresis – electrospray mass spectrometry for the characterization of differential oxidation in glycoproteins by charge reversal and protease/glycosidase digestion. Anal Chem 73:5875–5885

pubmed: 11791556 doi: 10.1021/ac0106748

Yang Y, Boysen RI, Matyska MT et al (2007) Open-tubular capillary electrochromatography coupled with electrospray ionization mass spectrometry for peptide analysis. Anal Chem 79:4942–4949

pubmed: 17539599 doi: 10.1021/ac0622633

Cheng J, Chen DDY (2018) Nonaqueous capillary electrophoresis mass spectrometry method for determining highly hydrophobic peptides. Electrophoresis 39:1216–1221. https://doi.org/10.1002/elps.201700364

pubmed: 28990192 doi: 10.1002/elps.201700364

Ruckenstein E, Shulgin IL (2006) Effect of salts and organic additives on the solubility of proteins in aqueous solutions. Adv Colloid Interface Sci 126:97–103. https://doi.org/10.1016/j.cis.2006.05.018

doi: 10.1016/j.cis.2006.05.018

Li F-A, Huang J-L, Her G-R (2008) Chip-CE/MS using a flat low-sheath-flow interface. Electrophoresis 29:4938–4943. https://doi.org/10.1002/elps.200800271

pubmed: 19130573 doi: 10.1002/elps.200800271

Li F-A, Huang J-L, Shen S-Y et al (2009) Development of a liquid-junction/low-flow interface for phosphate buffer capillary electrophoresis mass spectrometry. Anal Chem 81:2810–2814. https://doi.org/10.1021/ac802491y

pubmed: 19245229 doi: 10.1021/ac802491y

Tang Q, Hamata AK, Lee G (1995) Capillary isoelectric focusing-electrospray mass spectrometry for protein analysis. Anal Chem 67:3515–3519

doi: 10.1021/ac00115a021

Dai J, Lamp J, Xia Q, Zhang Y (2018) Capillary isoelectric focusing-mass spectrometry method for the separation and online characterization of intact monoclonal antibody charge variants. Anal Chem 90:2246–2254. https://doi.org/10.1021/acs.analchem.7b04608

pubmed: 29272582 doi: 10.1021/acs.analchem.7b04608

Kohl FJ, Montealegre C, Neusüß C (2016) On-line two-dimensional capillary electrophoresis with mass spectrometric detection using a fully electric isolated mechanical valve. Electrophoresis 37:954–958. https://doi.org/10.1002/elps.201500579

pubmed: 26799982 doi: 10.1002/elps.201500579 pmcid: 26799982

Schlecht J, Jooß K, Neusüß C (2018) Two-dimensional capillary electrophoresis-mass spectrometry (CE-CE-MS): coupling MS-interfering capillary electromigration methods with mass spectrometry. Anal Bioanal Chem 410:6353–6359

pubmed: 29862434 doi: 10.1007/s00216-018-1157-9

Moritz B, Schnaible V, Kiessig S et al (2015) Evaluation of capillary zone electrophoresis for charge heterogeneity testing of monoclonal antibodies. J Chromatogr B 983–984:101–110. https://doi.org/10.1016/j.jchromb.2014.12.024

doi: 10.1016/j.jchromb.2014.12.024

Jooß K, Hühner J, Kiessig S et al (2017) Two-dimensional capillary zone electrophoresis – mass spectrometry for the characterization of intact monoclonal antibody charge variants, including deamidation products. Anal Bioanal Chem 409:6057–6067. https://doi.org/10.1007/s00216-017-0542-0

pubmed: 28801824 doi: 10.1007/s00216-017-0542-0 pmcid: 28801824

Cifuentes A, Santos JM, Frutos MD (1993) High-efficiency capillary electrophoretic separation of basic proteins using coated capillaries and cationic buffer additives evaluation of protein-capillary wall interactions. J Chromatogr 652:161–170

doi: 10.1016/0021-9673(93)80656-S

Huhn C, Ramautar R, Wuhrer M, Somsen GW (2010) Relevance and use of capillary coatings in capillary electrophoresis – mass spectrometry. Anal Bioanal Chem 396:297–314. https://doi.org/10.1007/s00216-009-3193-y

pubmed: 19838682 doi: 10.1007/s00216-009-3193-y

Staub A, Comte S, Rudaz S et al (2010) Use of organic solvent to prevent protein adsorption in CE-MS experiments. Electrophoresis 31:3326–3333. https://doi.org/10.1002/elps.201000245

pubmed: 22216450 doi: 10.1002/elps.201000245

Moini M, Huang H (2004) Application of capillary electrophoresis/electrospray ionization-mass spectrometry to subcellular proteomics of Escherichia coli ribosomal proteins. Electrophoresis 25:1981–1987. https://doi.org/10.1002/elps.200305906

pubmed: 15237397 doi: 10.1002/elps.200305906

Simó C, Herrero M, Neusüß C et al (2005) Characterization of proteins from Spirulina platensis microalga using capillary electrophoresis-ion trap-mass spectrometry and capillary electrophoresis-time of flight-mass spectrometry. Electrophoresis 26:2674–2683. https://doi.org/10.1002/elps.200500055

pubmed: 15929060 doi: 10.1002/elps.200500055

Martin GB, Mansion F, Servais A-C et al (2009) CE-MS method development for peptides analysis, especially hepcidin, an iron metabolism marker. Electrophoresis 30:2624–2631. https://doi.org/10.1002/elps.200800794

pubmed: 19621376 doi: 10.1002/elps.200800794

Porras SP, Kenndler E (2005) Are the asserted advantages of organic solvents in capillary electrophoresis real? A critical discussion. Electrophoresis 26:3203–3220. https://doi.org/10.1002/elps.200500311

pubmed: 16143976 doi: 10.1002/elps.200500311

Lucy CA, Macdonald AM, Gulcev MD (2008) Non-covalent capillary coatings for protein separations in capillary electrophoresis. J Chromatogr 1184:81–105. https://doi.org/10.1016/j.chroma.2007.10.114

doi: 10.1016/j.chroma.2007.10.114

Pattky M, Barkovits K, Marcus K et al (2016) Statically adsorbed coatings for high separation efficiency and resolution in CE – MS peptide analysis: strategies and implementation. In: Capillary electrophoresis: methods and protocols. Humana Press, New York, NY, pp 53–75. https://doi.org/10.1007/978-1-4939-6403-1

Ciccone B (2001) A buffer system for capillary electrophoresis. Am Lab 33:30–33

Giorgio P, Gelfi C, Sebastiano R, Citterio A (2004) Surfing silica surfaces superciliously. J Chromatogr 1053:15–26. https://doi.org/10.1016/j.chroma.2004.05.073

doi: 10.1016/j.chroma.2004.05.073

Nguyen TTTN, Petersen NJ, Rand KD (2016) A simple sheathless CE-MS interface with a sub-micrometer electrical contact fracture for sensitive analysis of peptide and protein samples. Anal Chim Acta 936:157–167. https://doi.org/10.1016/j.aca.2016.07.002

pubmed: 27566351 doi: 10.1016/j.aca.2016.07.002

Huck CW, Bakry R, Huber LA, Bonn GK (2006) Progress in capillary electrophoresis coupled to matrix-assisted laser desorption/ionization – time of flight mass spectrometry. Electrophoresis 27:2063–2074. https://doi.org/10.1002/elps.200600046

pubmed: 16645982 doi: 10.1002/elps.200600046

Zaia J (2014) Capillary electrophoresis-mass spectrometry of carbohydrates. Methods Mol Biol:13–25. https://doi.org/10.1007/978-1-62703-296-4

Gahoual R, Beck A, Leize-wagner E, Franc Y (2016) Cutting-edge capillary electrophoresis characterization of monoclonal antibodies and related products. J Chromatogr B 1032:61–78. https://doi.org/10.1016/j.jchromb.2016.05.028

doi: 10.1016/j.jchromb.2016.05.028

Týčová A, Ledvina V, Klepárník K (2017) Recent advances in CE-MS coupling: instrumentation, methodology, and applications. Electrophoresis 38:115–134. https://doi.org/10.1002/elps.201600366

pubmed: 27783411 doi: 10.1002/elps.201600366 pmcid: 27783411

Krenkova J, Kleparnik K, Luksch J, Foret F (2019) Microfabricated liquid junction hybrid capillary electrophoresis-mass spectrometry interface for fully automated operation. Electrophoresis:1–20. https://doi.org/10.1002/elps.201900049

Bodnar J, Hajba L, Guttman A (2016) A fully automated linear polyacrylamide coating and regeneration method for capillary electrophoresis of proteins. Electrophoresis 37:3154–3159. https://doi.org/10.1002/elps.201600405

pubmed: 27731499 doi: 10.1002/elps.201600405

Zhang Z, Dovichi NJ (2018) Optimization of mass spectrometric parameters improve the identification performance of capillary zone electrophoresis for single-shot bottom-up proteomics analysis. Anal Chim Acta 1001:93–99. https://doi.org/10.1016/j.aca.2017.11.023

pubmed: 29291811 doi: 10.1016/j.aca.2017.11.023

Stutz H (2009) Protein attachment onto silica surfaces – a survey of molecular fundamentals, resulting effects and novel preventive strategies in CE. Electrophoresis 30:2032–2061. https://doi.org/10.1002/elps.200900015

pubmed: 19582707 doi: 10.1002/elps.200900015

Volpi N, Maccari F (2009) Capillary electrophoresis of biomolecules: methods and protocols. Humana Press, New York, NY

Höcker O, Montealegre C, Neusüß C (2018) Characterization of a nanoflow sheath liquid interface and comparison to a sheath liquid and a sheathless porous-tip interface for CE-ESI-MS in positive and negative ionization. Anal Bioanal Chem 410:5265–5275. https://doi.org/10.1007/s00216-018-1179-3

pubmed: 29943266 doi: 10.1007/s00216-018-1179-3

Xia JQ (2016) Coated capillaries for CE-MS of therapeutic protein. In: Capillary electrophoresis–mass spectrometry. Springer, Cham, pp 7–12

doi: 10.1007/978-3-319-46240-0_2

Hernández-Borges J, Neusüß C, Cifuentes A, Pelzing M (2004) On-line capillary electrophoresis-mass spectrometry for the analysis of biomolecules. Electrophoresis 25:2257–2281. https://doi.org/10.1002/elps.200405954

pubmed: 15274009 doi: 10.1002/elps.200405954 pmcid: 15274009

Stutz H (2005) Advances in the analysis of proteins and peptides by capillary electrophoresis with matrix-assisted laser desorption/ionization and electrospray-mass spectrometry detection. Electrophoresis 26:1254–1290. https://doi.org/10.1002/elps.200410130

pubmed: 15776483 doi: 10.1002/elps.200410130 pmcid: 15776483

Khatri K, Klein JA, Haserick JR et al (2018) Microfluidic capillary electrophoresis–mass spectrometry for analysis of monosaccharides, oligosaccharides, and glycopeptides. Anal Chem 89:6645–6655. https://doi.org/10.1021/acs.anal-chem.7b00875.Detailed

doi: 10.1021/acs.analchem.7b00875

Moreno-Gonz D, Laura G, Garc AM, Somsen GW (2013) Micellar electrokinetic chromatography – electrospray ionization mass spectrometry employing a volatile surfactant for the analysis of amino acids in human urine. Electrophoresis 34:2615–2622. https://doi.org/10.1002/elps.201300247

doi: 10.1002/elps.201300247

Elhamili A, Wetterhall M, Arvidsson B et al (2008) Rapid capillary electrophoresis time-of-flight mass spectrometry separations of peptides and proteins using a monoquaternarized piperazine compound (M7C4I) for capillary coatings. Electrophoresis 29:1619–1625. https://doi.org/10.1002/elps.200700737

pubmed: 18383015 doi: 10.1002/elps.200700737 pmcid: 18383015

Bhardwaj C, Hanley L (2014) Ion sources for mass spectrometric identification and imaging of molecular species. Nat Prod Rep 31:756–767. https://doi.org/10.1039/c3np70094a

pubmed: 24473154 doi: 10.1039/C3NP70094A pmcid: 24473154

Marginean I, Kelly RT, Prior DC et al (2008) Analytical characterization of the electrospray ion source in the nanoflow regime. Anal Chem 80:6573–6579

pubmed: 18661954 pmcid: 2692497 doi: 10.1021/ac800683s

Moini M (2007) Simplifying CE – MS operation. 2. Interfacing low-flow separation techniques to mass spectrometry using a porous tip. Anal Chem 79:4241–4246

pubmed: 17447730 doi: 10.1021/ac0704560

Bonvin G, Rudaz S, Schappler J (2014) In-spray supercharging of intact proteins by capillary electrophoresis – electrospray ionization – mass spectrometry using sheath liquid interface. Anal Chim Acta 813:97–105. https://doi.org/10.1016/j.aca.2013.12.043

pubmed: 24528666 doi: 10.1016/j.aca.2013.12.043

Krenkova J, Kleparnik K, Grym J et al (2016) Self-aligning subatmospheric hybrid liquid junction electrospray interface for capillary electrophoresis. Electrophoresis 37:414–417. https://doi.org/10.1002/elps.201500357

pubmed: 26331678 doi: 10.1002/elps.201500357 pmcid: 26331678

Fanali C, Orazio GD, Fanali S (2012) Nano-liquid chromatography and capillary electrochromatography hyphenated with mass spectrometry for tryptic digest protein analysis: a comparison. Electrophoresis 33:2553–2560. https://doi.org/10.1002/elps.201200157

pubmed: 22899263 doi: 10.1002/elps.201200157 pmcid: 22899263

Wojcik R, Dada OO, Sadilek M, Dovichi NJ (2010) Simplified capillary electrophoresis nanospray sheath- flow interface for high efficiency and sensitive peptide analysis. Rapid Commun Mass Spectrom 24:2554–2560

pubmed: 20740530 doi: 10.1002/rcm.4672 pmcid: 20740530

Sun L, Zhu G, Zhao Y et al (2013) Ultrasensitive and fast bottom-up analysis of femtogram amounts of complex proteome digests. Angew Chemie 52:13661–13664. https://doi.org/10.1002/anie.201308139

doi: 10.1002/anie.201308139

Sun L, Zhu G, Zhang Z et al (2015) Third-generation electrokinetically pumped sheath-flow nanospray interface with improved stability and sensitivity for automated capillary zone electrophoresis − mass spectrometry analysis of complex proteome digests. J Proteome Res 14:2312–2321. https://doi.org/10.1021/acs.jproteome.5b00100

pubmed: 25786131 pmcid: 4416984 doi: 10.1021/acs.jproteome.5b00100

Qu Y, Sun L, Zhu G et al (2018) Sensitive and fast characterization of site-specific protein glycosylation with capillary electrophoresis coupled to mass spectrometry. Talanta 179:22–27. https://doi.org/10.1016/j.talanta.2017.10.015

pubmed: 29310225 doi: 10.1016/j.talanta.2017.10.015 pmcid: 29310225

Johnson RT, To NH, Stobaugh JF, Lunte CE (2017) The development of a Sheathless Interface for capillary electrophoresis electrospray ionization mass spectrometry using a cellulose acetate cast capillary. Chromatographia 80:1061–1067. https://doi.org/10.1007/s10337-017-3326-y

doi: 10.1007/s10337-017-3326-y

Tycova A, Foret F (2015) Capillary electrophoresis in an extended nanospray tip – electrospray as an electrophoretic column. J Chromatogr A 1388:274–279. https://doi.org/10.1016/j.chroma.2015.02.042

pubmed: 25736305 doi: 10.1016/j.chroma.2015.02.042 pmcid: 25736305

Haselberg R, Ratnayake CK, Jong GJD, Somsen GW (2010) Performance of a sheathless porous tip sprayer for capillary electrophoresis – electrospray ionization-mass spectrometry of intact proteins. J Chromatogr A 1217:7605–7611. https://doi.org/10.1016/j.chroma.2010.10.006

pubmed: 20970804 doi: 10.1016/j.chroma.2010.10.006 pmcid: 20970804

Heemskerk AAM, Deelder M, Mayboroda OA (2014) CE–ESI-MS for bottom-up proteomics: advances in separation, interfacing and applications. Mass Spectrom Rev 35:259–271. https://doi.org/10.1002/mas

pubmed: 24852088 doi: 10.1002/mas.21432 pmcid: 24852088

Heemskerk AAM, Busnel J, Schoenmaker B et al (2012) Ultra-low flow electrospray ionization-mass spectrometry for improved ionization efficiency in phosphoproteomics. Anal Chem 84:4552–4559. https://doi.org/10.1021/ac300641x

pubmed: 22494114 doi: 10.1021/ac300641x

Dominguez-Vega E, De Vijlder T, Romijn EP, Somsen GW (2017) Capillary electrophoresis-tandem mass spectrometry as a highly selective tool for the compositional and site-specific assessment of multiple peptide-deamidation. Anal Chim Acta 982:122–130. https://doi.org/10.1016/j.aca.2017.06.021

pubmed: 28734351 doi: 10.1016/j.aca.2017.06.021

Jarvas G, Fonslow B, Iii JRY et al (2017) Characterization of a porous nano-electrospray capillary emitter at ultra-low flow rates. J Chromatogr Sci 55:47–51. https://doi.org/10.1093/chromsci/bmw148

pubmed: 27993863 doi: 10.1093/chromsci/bmw148

Haselberg R, de Jong GJ, Somsen GW (2013) Low-flow sheathless capillary electrophoresis–mass spectrometry for sensitive glycoform profiling of intact pharmaceutical proteins. Anal Chem 85:2289–2296. https://doi.org/10.1021/ac303158f

pubmed: 23323765 doi: 10.1021/ac303158f

Kammeijer GSM, Kohler I, Jansen BC et al (2016) Dopant enriched nitrogen gas combined with sheathless capillary electrophoresis − electrospray ionization-mass spectrometry for improved sensitivity and repeatability in glycopeptide analysis. Anal Chem 88:5849–5856. https://doi.org/10.1021/acs.analchem.6b00479

pubmed: 27119460 doi: 10.1021/acs.analchem.6b00479

Busnel J, Josserand J, Lion N, Girault HH (2009) Iontophoretic fraction collection for coupling capillary zone electrophoresis with matrix-assisted laser desorption/ionization mass spectrometry. Anal Chem 81:3867–3872

pubmed: 19374373 doi: 10.1021/ac900128q

Romson J, Jacksén J, Emmer Å (2019) An automated system for CE-MALDI and on-target digestion under a fluorocarbon lid applied on spermatophore proteins from Pieris napi. J Chromatogr B 1104:228–233. https://doi.org/10.1016/j.jchromb.2018.11.021

doi: 10.1016/j.jchromb.2018.11.021

Biacchi M, Said N, Beck A, Leize-wagner E (2017) Top-down and middle-down approach by fraction collection enrichment using off-line capillary electrophoresis – mass spectrometry coupling: application to monoclonal antibody F c/2 charge variants. J Chromatogr A 1498:120–127. https://doi.org/10.1016/j.chroma.2017.02.064

pubmed: 28259456 doi: 10.1016/j.chroma.2017.02.064

Johnson T, Bergquist J, Ekman R et al (2001) A CE-MALDI interface based on the use of prestructured sample supports. Anal Chem 73:2278–2283. https://doi.org/10.1021/ac0011888

Rejtar T, Hu P, Juhasz P et al (2002) Off-line coupling of high-resolution capillary electrophoresis to MALDI-TOF and TOF/TOF MS. J Proteome Res 1:171–179. https://doi.org/10.1021/pr015519o

pubmed: 12643537 doi: 10.1021/pr015519o

Preisler J, Foret F, Karger BL (1998) On-line MALDI-TOF MS using a continuous vacuum deposition interface. Anal Chem 70:5278–5287. https://doi.org/10.1021/ac9807823

pubmed: 9868918 doi: 10.1021/ac9807823

Musyimi HK, Narcisse DA, Zhang X et al (2004) Online CE – MALDI-TOF MS using a rotating ball interface. Anal Chem 76:5968–5973. https://doi.org/10.1021/ac0489723

pubmed: 15456323 doi: 10.1021/ac0489723

Rogowska A, Pomastowski P, Złoch M, Viorica R (2018) The influence of different pH on the electrophoretic behaviour of Saccharomyces cerevisiae modified by calcium ions. Sci Rep 8:2–11. https://doi.org/10.1038/s41598-018-25024-4

doi: 10.1038/s41598-018-25024-4

Mann M, Kelleher NL (2008) Precision proteomics: the case for high resolution and high mass accuracy. Proc Natl Acad Sci U S A 105:18132–18138. https://doi.org/10.1073/pnas.0800788105

pubmed: 18818311 pmcid: 2587563 doi: 10.1073/pnas.0800788105

Shen Y, Jacobs JM, Camp DG I et al (2004) Ultra-high-efficiency strong cation exchange LC/RPLC/MS/MS for high dynamic range characterization of the human plasma proteome. Anal Chem 76(4):1134–1144. https://doi.org/10.1021/AC034869M

Guthals A, Bandeira N (2012) Peptide identification by tandem mass spectrometry with alternate fragmentation modes. Mol Cell Proteomics 11:550–557. https://doi.org/10.1074/mcp.R112.018556

pubmed: 22595789 pmcid: 3434779 doi: 10.1074/mcp.R112.018556

Zürbig P, Renfrow MB, Schiffer E et al (2006) Biomarker discovery by CE-MS enables sequence analysis via MS/MS with platform-independent separation. Electrophoresis 27:2111–2125. https://doi.org/10.1002/elps.200500827

pubmed: 16645980 doi: 10.1002/elps.200500827

Li Y, Compton PD, Tran JC et al (2014) Optimizing capillary electrophoresis for top-down proteomics of 30–80 kDa proteins. Proteomics 14:1158–1164. https://doi.org/10.1002/pmic.201300381

pubmed: 24596178 pmcid: 4034378 doi: 10.1002/pmic.201300381

Zhao Y, Sun L, Champion MM et al (2014) Capillary zone electrophoresis–electrospray ionization-tandem mass spectrometry for top-down characterization of the Mycobacterium marinum secretome. Anal Chem 86:4873–4878. https://doi.org/10.1021/ac500092q

pubmed: 24725189 pmcid: 4033641 doi: 10.1021/ac500092q

Sun L, Knierman MD, Zhu G, Dovichi NJ (2013) Fast top-down intact protein characterization with capillary zone electrophoresis–electrospray ionization tandem mass spectrometry. Anal Chem 85:5989–5995. https://doi.org/10.1021/ac4008122

pubmed: 23692435 pmcid: 3770260 doi: 10.1021/ac4008122

Han X, Wang Y, Aslanian A et al (2014) Sheathless capillary electrophoresis-tandem mass spectrometry for top-down characterization of Pyrococcus furiosus proteins on a proteome scale. Anal Chem 86:11006–11012. https://doi.org/10.1021/ac503439n

pubmed: 25346219 pmcid: 4238646 doi: 10.1021/ac503439n

Han X, Wang Y, Aslanian A et al (2014) In-line separation by capillary electrophoresis prior to analysis by top-down mass spectrometry enables sensitive characterization of protein complexes. J Proteome Res 13:6078–6086. https://doi.org/10.1021/pr500971h

pubmed: 25382489 pmcid: 4262260 doi: 10.1021/pr500971h

Zhao Y, Riley NM, Sun L et al (2015) Coupling capillary zone electrophoresis with electron transfer dissociation and activated ion electron transfer dissociation for top-down proteomics. Anal Chem 87:5422–5429. https://doi.org/10.1021/acs.analchem.5b00883

pubmed: 25893372 pmcid: 4439324 doi: 10.1021/acs.analchem.5b00883

Pontillo C, Filip S, Borràs DM et al (2015) CE-MS-based proteomics in biomarker discovery and clinical application. Proteomics Clin Appl 9:322–334. https://doi.org/10.1002/prca.201400115

pubmed: 25641774 doi: 10.1002/prca.201400115 pmcid: 25641774

Robledo VR, Smyth WF (2014) Review of the CE-MS platform as a powerful alternative to conventional couplings in bio-omics and target-based applications. Electrophoresis 35:2292–2308. https://doi.org/10.1002/elps.201300561

pubmed: 24488766 doi: 10.1002/elps.201300561

Stolz A, Jooß K, Oliver H et al (2019) Recent advances in capillary electrophoresis- mass spectrometry: instrumentation, methodology and applications. Electrophoresis 40:79–112. https://doi.org/10.1002/elps.201800331

pubmed: 30260009 doi: 10.1002/elps.201800331 pmcid: 30260009

Haselberg R, de Jong GJ, Somsen GW (2013) CE-MS for the analysis of intact proteins 2010–2012. Electrophoresis:99–112. https://doi.org/10.1002/elps.201200439

Jiang Y, He MY, Zhang WJ et al (2017) Recent advances of capillary electrophoresis-mass spectrometry instrumentation and methodology. Chin Chem Lett 28:1640–1652. https://doi.org/10.1016/j.cclet.2017.05.008

doi: 10.1016/j.cclet.2017.05.008

Faserl K, Sarg B, Maurer V, Lindner HH (2017) Exploiting charge differences for the analysis of challenging post-translational modifications by capillary electrophoresis-mass spectrometry. J Chromatogr A 1498:215–223. https://doi.org/10.1016/j.chroma.2017.01.086

pubmed: 28179079 doi: 10.1016/j.chroma.2017.01.086 pmcid: 28179079

Steen H, Jebanathirajah JA, Rush J et al (2006) Phosphorylation analysis by mass spectrometry. Mol Cell Proteomics 5:172–181. https://doi.org/10.1074/mcp.M500135-MCP200

pubmed: 16204703 doi: 10.1074/mcp.M500135-MCP200 pmcid: 16204703

Faserl K, Sarg B, Gruber P, Lindner HH (2018) Investigating capillary electrophoresis-mass spectrometry for the analysis of common post-translational modifications. Electrophoresis:1–8. https://doi.org/10.1002/elps.201700437

Mou S, Sun L, Dovichi NJ (2014) Accurate determination of peptide phosphorylation stoichiometry via automated diagonal capillary electrophoresis coupled with mass spectrometry – proof of principle. Anal Chem 85:10692–10696. https://doi.org/10.1021/ac402858a.Accurate

doi: 10.1021/ac402858a

Svozil J, Baerenfaller K (2017) A cautionary tale on the inclusion of variable posttranslational modifications in database-dependent searches of mass spectrometry data. Methods Enzymol 586:433–452. https://doi.org/10.1016/BS.MIE.2016.11.007

pubmed: 28137575 doi: 10.1016/bs.mie.2016.11.007

Robinson NE, Robinson AB (2001) Molecular clocks. Proc Natl Acad Sci 98:944–949. https://doi.org/10.1073/PNAS.98.3.944

pubmed: 11158575 pmcid: 14689 doi: 10.1073/pnas.98.3.944

Hains PG, Truscott RJW (2010) Age-dependent deamidation of lifelong proteins in the human lens. Invest Opthalmol Vis Sci 51:3107. https://doi.org/10.1167/iovs.09-4308

doi: 10.1167/iovs.09-4308

Pace AL, Wong RL, Zhang YT et al (2013) Asparagine deamidation dependence on buffer type, pH, and temperature. J Pharm Sci 102:1712–1723. https://doi.org/10.1002/jps.23529

pubmed: 23568760 doi: 10.1002/jps.23529

Zheng JY, Janis LJ (2006) Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298. Int J Pharm 308:46–51. https://doi.org/10.1016/J.IJPHARM.2005.10.024

pubmed: 16316730 doi: 10.1016/j.ijpharm.2005.10.024

Gervais D (2016) Protein deamidation in biopharmaceutical manufacture: understanding, control and impact. J Chem Technol Biotechnol 91:569–575. https://doi.org/10.1002/jctb.4850

doi: 10.1002/jctb.4850

Rosnack KJ, Stroh JG, Singleton DH et al (1994) Use of capillary electrophoresis-electrospray ionization mass spectrometry in the analysis of synthetic peptides. J Chromatogr A 675:219–225. https://doi.org/10.1016/0021-9673 (94)85275-8

pubmed: 8081459 doi: 10.1016/0021-9673(94)85275-8 pmcid: 8081459

Coon JJ, Zürbig P, Dakna M et al (2008) CE-MS analysis of the human urinary proteome for biomarker discovery and disease diagnostics. Proteomics Clin Appl 2:964–973. https://doi.org/10.1002/prca.200800024

pubmed: 20130789 pmcid: 2815342 doi: 10.1002/prca.200800024

Gahoual R, Beck A, François Y-N, Leize-Wagner E (2016) Independent highly sensitive characterization of asparagine deamidation and aspartic acid isomerization by sheathless CZE-ESI-MS/MS. J Mass Spectrom 51:150–158. https://doi.org/10.1002/jms.3735

pubmed: 26889931 doi: 10.1002/jms.3735 pmcid: 26889931

Gennaro LA, Salas-Solano O (2009) Characterization of deamidated peptide variants by micro-preparative capillary electrophoresis and mass spectrometry. J Chromatogr A 1216:4499–4503. https://doi.org/10.1016/j.chroma.2009.03.025

pubmed: 19342060 doi: 10.1016/j.chroma.2009.03.025 pmcid: 19342060

Bush DR, Zang L, Belov AM et al (2016) High resolution CZE-MS quantitative characterization of intact biopharmaceutical proteins: proteoforms of interferon-β1. Anal Chem 88:1138–1146. https://doi.org/10.1021/acs.analchem.5b03218

pubmed: 26641950 doi: 10.1021/acs.analchem.5b03218 pmcid: 26641950

Staub A, Giraud S, Saugy M et al (2010) CE-ESI-TOF/MS for human growth hormone analysis. Electrophoresis 31:388–395. https://doi.org/10.1002/elps.200900315

pubmed: 20024916 doi: 10.1002/elps.200900315 pmcid: 20024916

Taichrib A, Pelzing M, Pellegrino C et al (2011) High resolution TOF MS coupled to CE for the analysis of isotopically resolved intact proteins. J Proteomics 74:958–966. https://doi.org/10.1016/J.JPROT.2011.01.006

pubmed: 21272675 doi: 10.1016/j.jprot.2011.01.006 pmcid: 21272675

Bergström T, Fredriksson S-Å, Nilsson C, Åstot C (2015) Deamidation in ricin studied by capillary zone electrophoresis- and liquid chromatography–mass spectrometry. J Chromatogr B 974:109–117. https://doi.org/10.1016/J.JCHROMB.2014.10.015

doi: 10.1016/j.jchromb.2014.10.015

Redman EA, Mellors JS, Starkey JA, Ramsey JM (2016) Characterization of intact antibody drug conjugate variants using micro fluidic capillary electrophoresis − mass spectrometry. Anal Chem 88:2220–2226. https://doi.org/10.1021/acs.analchem.5b03866

pubmed: 26765745 doi: 10.1021/acs.analchem.5b03866 pmcid: 26765745

Kammeijer GSM, Jansen BC, Kohler I et al (2017) Sialic acid linkage differentiation of glycopeptides using capillary electrophoresis – electrospray ionization – mass spectrometry. Sci Rep:1–10. https://doi.org/10.1038/s41598-017-03838-y

Amon S, Zamfir AD, Rizzi A (2008) Glycosylation analysis of glycoproteins and proteoglycans using capillary electrophoresis-mass spectrometry strategies. Electrophoresis 29:2485–2507. https://doi.org/10.1002/elps.200800105

pubmed: 18512669 doi: 10.1002/elps.200800105 pmcid: 18512669

Zhang Q, Li Z, Wang Y et al (2017) Mass spectrometry for protein sialoglycosylation. Mass Spectrom Rev:1–29. https://doi.org/10.1002/mas.21555

Pompach P, Brnakova Z, Sanda M et al (2013) Site-specific glycoforms of haptoglobin in liver cirrhosis and hepatocellular carcinoma. Mol Cell Proteomics:1281–1293. https://doi.org/10.1074/mcp.M112.023259

Yang N, Goonatilleke E, Park D et al (2016) Quantitation of site-specific glycosylation in manufactured recombinant monoclonal antibody drugs. Anal Chem 88:7091–7100. https://doi.org/10.1021/acs.analchem.6b00963

pubmed: 27311011 pmcid: 4955800 doi: 10.1021/acs.analchem.6b00963

Nilsson J, Rüetschi U, Halim A et al (2009) Enrichment of glyco – peptides for glycan structure and attachment site identification. Nat Methods 6:809–811. https://doi.org/10.1038/nmeth.1392

pubmed: 19838169 pmcid: 19838169 doi: 10.1038/nmeth.1392

Hu H, Khatri K, Klein J et al (2016) A review of methods for interpretation of glycopeptide tandem mass spectral data. Glycoconj J 33:285–296. https://doi.org/10.1007/s10719-015-9633-3

pubmed: 26612686 doi: 10.1007/s10719-015-9633-3 pmcid: 26612686

Hinneburg H, Stavenhagen K, Schweiger-hufnagel U et al (2015) The art of destruction: optimizing collision energies. J Am Soc Mass Spectrom 27:507–519. https://doi.org/10.1007/s13361-015-1308-6

doi: 10.1007/s13361-015-1308-6

Amon S, Plematl A, Rizzi A (2006) Capillary zone electrophoresis of glycopeptides under controlled electroosmotic flow conditions coupled to electrospray and matrix-assisted laser desorption/ionization mass spectrometry. Electrophoresis 27:1209–1219. https://doi.org/10.1002/elps.200500725

pubmed: 16523459 doi: 10.1002/elps.200500725

Schönemeier B, Metzger J, Klein J et al (2016) Urinary peptide analysis differentiates pancreatic cancer from chronic pancreatitis. Pancreas 00:1–9

Wittke S, Mischak H, Walden M et al (2005) Discovery of biomarkers in human urine and cerebrospinal fluid by capillary electrophoresis coupled to mass spectrometry: towards new. Electrophoresis 3:1476–1487. https://doi.org/10.1002/elps.200410140

doi: 10.1002/elps.200410140

Haselberg R, Vijlder TD, Heukers R et al (2018) Heterogeneity assessment of antibody-derived therapeutics at the intact and middle-up level by low-flow sheathless capillary electrophoresis-mass spectrometry. Anal Chim Acta 1044:181–190. https://doi.org/10.1016/j.aca.2018.08.024

pubmed: 30442400 doi: 10.1016/j.aca.2018.08.024

Gahoual R, Houzé P, François YN (2018) Revealing the potential of capillary electrophoresis/mass spectrometry: the tipping point. 1–9 . https://doi.org/10.1002/rcm.8238

Giménez E, Ramos-Hernan R, Benavente F et al (2012) Analysis of recombinant human erythropoietin glycopeptides by capillary electrophoresis electrospray – time of flight-mass spectrometry. Anal Chim Acta 709:81–90. https://doi.org/10.1016/j.aca.2011.10.028

pubmed: 22122935 doi: 10.1016/j.aca.2011.10.028 pmcid: 22122935

Said N, Gahoual R, Kuhn L et al (2016) Structural characterization of antibody drug conjugate by a combination of intact, middle-up and bottom-up techniques using sheathless capillary electrophoresis – tandem mass spectrometry as nanoESI infusion platform and separation method. Anal Chim Acta 918:50–59. https://doi.org/10.1016/j.aca.2016.03.006

pubmed: 27046210 doi: 10.1016/j.aca.2016.03.006 pmcid: 27046210

Wakankar A, Chen Y, Gokarn Y, Jacobson FS (2011) Analytical methods for physicochemical characterization of antibody drug conjugates. MAbs 3:161–172. https://doi.org/10.4161/mabs.3.2.14960

pubmed: 21441786 pmcid: 3092617 doi: 10.4161/mabs.3.2.14960

Han M, Pearson JT, Wang Y et al (2017) Immunoaffinity capture coupled with capillary electrophoresis – mass spectrometry to study therapeutic protein stability in vivo. Anal Biochem 539:118–126. https://doi.org/10.1016/j.ab.2017.10.005

pubmed: 29029979 doi: 10.1016/j.ab.2017.10.005 pmcid: 29029979

Han M, Rock BM, Pearson JT, Rock DA (2016) Intact mass analysis of monoclonal antibodies by capillary electrophoresis — mass spectrometry. J Chromatogr B 1011:24–32. https://doi.org/10.1016/j.jchromb.2015.12.045

doi: 10.1016/j.jchromb.2015.12.045

Giorgetti J, Lechner A, Nero ED, Beck A (2018) Intact monoclonal antibodies separation and analysis by sheathless capillary electrophoresis-mass spectrometry. Eur J Mass Spectrom:1–9. https://doi.org/10.1177/1469066718807798

Wenz C, Barbas C, López-Gonzálvez Á et al (2015) Interlaboratory study to evaluate the robustness of capillary electrophoresis-mass spectrometry for peptide mapping. J Sep Sci 38:3262–3270. https://doi.org/10.1002/jssc.201500551

pubmed: 26147246 doi: 10.1002/jssc.201500551

Metzger J, Mullen W, Husi H et al (2016) Acute kidney injury prediction in cardiac surgery patients by a urinary peptide pattern: a case-control validation study. Crit Care 20:157. https://doi.org/10.1186/s13054-016-1344-z

pubmed: 27230659 pmcid: 4882859 doi: 10.1186/s13054-016-1344-z

Markoska K, Pejchinovski M, Pontillo C et al (2018) Urinary peptide biomarker panel associated with an improvement in estimated glomerular filtration rate in chronic kidney disease patients. Nephrol Dial Transplant 33:751–759. https://doi.org/10.1093/ndt/gfx263

pubmed: 28992073 doi: 10.1093/ndt/gfx263 pmcid: 28992073

Albalat A, Husi H, Siwy J et al (2014) Capillary electrophoresis interfaced with a mass spectrometer (CE-MS): technical considerations and applicability for biomarker studies in animals. Curr Protein Pept Sci 15:23–35. https://doi.org/10.2174/1389203715666140221123920

pubmed: 24555889 doi: 10.2174/1389203715666140221123920 pmcid: 24555889

Pejchinovski M, Siwy J, Mullen W et al (2018) Urine peptidomic biomarkers for diagnosis of patients with systematic lupus erythematosus. Lupus 27:6–16. https://doi.org/10.1177/0961203317707827

pubmed: 28474961 doi: 10.1177/0961203317707827 pmcid: 28474961

Belczacka I, Latosinska A, Siwy J et al (2018) Urinary CE-MS peptide marker pattern for detection of solid tumors. Sci Rep 8:1–11. https://doi.org/10.1038/s41598-018-23585-y

doi: 10.1038/s41598-018-23585-y

Pontillo C, Mischak H (2017) Urinary peptide-based classifier CKD273: towards clinical application in chronic kidney disease. Clin Kidney J 10:192–201. https://doi.org/10.1093/ckj/sfx002

pubmed: 28694965 pmcid: 5499684 doi: 10.1093/ckj/sfx002

Rossing K, Bosselmann HS, Gustafsson F et al (2016) Urinary proteomics pilot study for biomarker discovery and diagnosis in heart failure with reduced ejection fraction. PLoS One 11:1–15. https://doi.org/10.1371/journal.pone.0157167

doi: 10.1371/journal.pone.0157167

Kammeijer GSM, Nouta J, De La Rosette JJMCH et al (2018) An in-depth glycosylation assay for urinary prostate-specific antigen. Anal Chem 90:4414–4421. https://doi.org/10.1021/acs.analchem.7b04281

pubmed: 29502397 pmcid: 5885261 doi: 10.1021/acs.analchem.7b04281

Zürbig P, Jahn H (2012) Use of proteomic methods in the analysis of human body fluids in Alzheimer research. Electrophoresis 33:3617–3630. https://doi.org/10.1002/elps.201200360

pubmed: 23160951 doi: 10.1002/elps.201200360

Rossetti DV, Martelli C, Longhi R et al (2013) Quantitative analysis of thymosin β4 in whole saliva by capillary electrophoresis-mass spectrometry using multiple ions monitoring (CE-MIM-MS). Electrophoresis 34:2674–2682. https://doi.org/10.1002/elps.201300165

pubmed: 23857244 doi: 10.1002/elps.201300165 pmcid: 23857244

Neuhaus J, Schiffer E, von Wilcke P et al (2013) Seminal plasma as a source of prostate cancer peptide biomarker candidates for detection of indolent and advanced disease. PLoS One 8. https://doi.org/10.1371/journal.pone.0067514

Lankisch TO, Metzger J, Negm AA et al (2011) Bile proteomic profiles differentiate cholangiocarcinoma from primary sclerosing cholangitis and choledocholithiasis. Hepatology 53:875–884. https://doi.org/10.1002/hep.24103

pubmed: 21374660 doi: 10.1002/hep.24103 pmcid: 21374660

Di Venere M, Viglio S, Cagnone M et al (2018) Advances in the analysis of “less-conventional” human body fluids: an overview of the CE- and HPLC-MS applications in the years 2015–2017. Electrophoresis 39:160–178. https://doi.org/10.1002/elps.201700276

pubmed: 28792066 doi: 10.1002/elps.201700276 pmcid: 28792066

Tu C, Rudnick PA, Martinez MY et al (2010) Depletion of abundant plasma proteins and limitations of plasma proteomics. J Proteome Res 9:4982–4991. https://doi.org/10.1021/pr100646w

pubmed: 20677825 pmcid: 2948641 doi: 10.1021/pr100646w

Stalmach A, Husi H, Mosbahi K, Albalat A, Mullen W, Mischak H (2015) Methods in capillary electrophoresis coupled to mass spectrometry for the identification of clinical proteomic/peptidomic biomarkers in biofluids. Methods Mol Biol 1243:187–205

pubmed: 25384747 doi: 10.1007/978-1-4939-1872-0_11 pmcid: 25384747

Engel N, Weiss VU, Wenz C et al (2015) Challenges of glycoprotein analysis by microchip capillary gel electrophoresis. Electrophoresis 36:1754–1758. https://doi.org/10.1002/elps.201400510

pubmed: 25931050 doi: 10.1002/elps.201400510 pmcid: 25931050

Herwig E, Marchetti-Deschmann M, Wenz C et al (2015) Sensitive detection of C-reactive protein in serum by immunoprecipitation–microchip capillary gel electrophoresis. Anal Biochem 478:102–106. https://doi.org/10.1016/J.AB.2015.03.009

pubmed: 25778394 doi: 10.1016/j.ab.2015.03.009 pmcid: 25778394

Dawod M, Kennedy RT, Arvin NE (2017) Recent advances in protein analysis by capillary and microchip electrophoresis. Analyst 142:1847–1866. https://doi.org/10.1039/c7an00198c

pubmed: 28470231 pmcid: 5516626 doi: 10.1039/C7AN00198C

Bertoletti L, Schappler J, Colombo R et al (2016) Evaluation of capillary electrophoresis-mass spectrometry for the analysis of the conformational heterogeneity of intact proteins using beta 2 -microglobulin as model compound. Anal Chim Acta 945:102–109. https://doi.org/10.1016/j.aca.2016.10.010

pubmed: 27968711 doi: 10.1016/j.aca.2016.10.010 pmcid: 27968711

Lombard-Banek C, Moody SA, Manzini MC, Nemes P (2019) Microsampling capillary electrophoresis mass spectrometry enables single-cell proteomics in complex tissues: developing cell clones in live Xenopus laevis and Zebrafish embryos. Anal Chem 91:4797–4805. https://doi.org/10.1021/acs.analchem.9b00345

pubmed: 30827088 pmcid: 6688183 doi: 10.1021/acs.analchem.9b00345

He M, Luo P, Hong J et al (2019) Structural analysis of biomolecules through a combination of mobility capillary electrophoresis and mass spectrometry. ACS Omega 4:2377–2386. https://doi.org/10.1021/acsomega.8b03224

pubmed: 31459477 pmcid: 6648644 doi: 10.1021/acsomega.8b03224

CE-MS for Proteomics and Intact Protein Analysis.

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Valeriia O Kuzyk (VO)

Govert W Somsen (GW)

Rob Haselberg (R)

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