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511 results on '"Lingeman, H."'

7. Online magnetic bead dynamic protein-affinity selection coupled to LC-MS for the screening of pharmacologically active compounds

Author

Jonker, N., Kretschmer, A., Kool, J., Fernandez, A., Kloos, D., Krabbe, J.G., Lingeman, H., and Irth, H.

Subjects
Liquid chromatography -- Methods, Liquid chromatography -- Equipment and supplies, Mass spectrometry -- Methods, Mass spectrometry -- Equipment and supplies, Drugs -- Product/Service Evaluations, Drugs -- Methods, Drugs -- Equipment and supplies, Chemistry
Abstract

The online, selective isolation of protein-ligand complexes using cobalt(II)-coated paramagnetic affinity beads (PABs) and subsequent liquid chromatography-mass spectrometry (LC-MS) determination of specifically bound ligands is described. After in-solution incubation of an analyte mixture with His-tagged target proteins, protein-analyte complexes are mixed with the Co(II)-PABs and subsequently injected into an in-house built magnetic trapping device. Bioactive ligands bound to the protein-Co(II)-PABs are retained in the magnetic field of the trapping device while inactive compounds are removed by washing with a pH 7.4 buffer. Active ligands are online eluted toward the LC-MS system using a pH shift. In the final step of the procedure, the protein-Co(II)-PABs are flushed to waste by temporarily lowering the magnetic field. The proof-of-principle is demonstrated by using commercially available Co(II)-PABs in combination with the His-tagged human estrogen-receptor ligand-binding domain. The system is characterized with a number of estrogenic ligands and nonbinding pharmaceutical compounds. The affinities of the test compounds varied from the high micromolar to the subnanomolar range. Typical detection limits are in the range from 20 to 80 nmol/L. The system is able to identify binders in mixtures of compounds, with an analysis time of 9.5 min per mixture. The standard deviation over 24 h is 9%.

Published
2009

11. Trace analysis of proteins using postseparation solution-phase digestion and electrospray mass spectrometric detection of marker peptides

Author

Bruyneel, B., Hoos, J.S., Smoluch, M.T., Lingeman, H., Niessen, W.M.A., and Irth, H.

Subjects
Trace analysis -- Methods, Proteins -- Identification and classification, Mass spectrometry -- Methods, Chemistry
Abstract

Analytical methodologies for the absolute quantitation of proteins typically include a digest step often using trypsin as the proteolytic enzyme. In the majority of cases, offline and on-line digestion methods are implemented prior to an LC-MS analysis system, requiring a high sequence coverage for unambiguous protein identification. For proteins with a strong overlap in amino acid sequence, e.g., therapeutic proteins and their metabolites, it is essential to separate proteins prior to digestion and the subsequent electrospray mass spectrometry analysis of marker peptides. Here, we present an on-line postcolumn solution-phase digestion methodology that is based on the continuous infusion of the proteolytic enzyme pepsin downstream to the nano C18 reversed-phase column. Proteins are identified based on their retention time in combination with the detection of specific marker peptides formed in the postcolumn digest. The optimization of important parameters such as enzyme concentration, reaction time, and organic modifier concentration is described. We demonstrated that the continuous-flow solution-phase digest method can be coupled on-line to the reversed-phase gradient liquid chromatography separation of proteins. Detection limits obtained for five model proteins, detected as specific marker peptides with m/z values of 300-1000, range from 30 to 90 fmol, with a linear response up to 3 pmol.

Published
2007

16. Ligand-exchange detection of phosphorylated peptides using liquid chromatography electrospray mass spectrometry

Author

Krabbe, J.G., Lingeman, H., Niessen, W.M.A., and Irth, H.

Subjects
Mass spectrometry -- Research, Chemistry
Abstract

Electrospray ionization mass spectrometry (ESI-MS) is used to selectively detect analytes with a high affinity for metal ions. The detection method is based on the selective monitoring of a competing ligand at its specific m/z value that is released during the ligand-exchange reaction of a metal-ligand complex with analyte(s) eluting from a reversed-phase liquid chromatography column. The ligand-exchange reaction proceeds in a postcolumn reaction detection system placed prior to the inlet of the electrospray MS interface. The feasibility of metal affinity detection by ESI-MS is demonstrated using phosphorylated peptides and iron(III)methylcalcein blue as reactant, as a model system. Methylcalcein blue (MCB) released upon interaction with phosphorylated peptides is detected at m/z 278. The ligand-exchange detection is coupled to a C8 reversed-phase column to separate several nonphosphorylated enkephalins and the phosphorylated peptides pp60 c-src (P) and M2170. Detection limits of 2 [micro]M were obtained for pp60 c-src (P) and M2170. The linearity of the detection method is tested in the range of 2-80 [micro]mol/L phosphorylated compounds ([r.sup.2] = 0.9996), and a relative standard deviation of less than 8% (n = 3) for all MCB responses of the different concentrations of phosphorylated compounds was obtained. The presented method showed specificity for phosphorylated peptides and may prove a useful tool for studying other ligand-exchange reactions and metal-protein interactions.

Published
2003

29. Abstract of papers Pharmaceutical and Biomedica Analysis Meeting

Author

Beysens, A. J., Beuman, G. H., van der Heijden, J. J., Hoogtanders, K. E. J., Steijqer, O. M., Lingeman, H., Bosman, J., Ensing, K., Franke, J. P., Hartstra, J., de Zesuw, R. A., de Fluiter, P., Jansen, E. H. J. M., Hoebus, J., Yun, Li Ming, Hoogmartens, J., Janssen, P. S. L., Langenhuizen, M. H. J. M., Kaijser, G. P., Beijnen, J. H., Jeunink, E., Underberg, W. J. M., Khan, K., Paesen, J., Roets, E., Lorreyne, W., Van Rompaey, F., Woestenborghs, R., Heykants, J., Hendrix, C., De Beer, J., Crommen, J., Van den Bossche, W., Porqueras, E., Hooqmartens, J., van Gijn, R., Koks, C. H. W., Rosing, H., Spruijt, M. P. N., Meenhorst, P. L., Burger, P. M., van Tellingen, O., Thoithi, G., Van Schepdael, A., Herdewijn, P., Pauwels, C., Geuens, I., Cornelissen, L., Van Roosbroeck, D., Macken, E., Van Aerschot, A., Vendrig, D. E. M. M., Gout, E., van der Voorden, E. C., van Hulten, O. L. T., Wafelman, A. R., Hoefnagel, C. A., Witte, D. T., Ahnoff, M., Franke, J. -P., de Zeeuw, R. A., and Yongxin, Zhu

Published
1993
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47. Chromatography-mass spectrometry based analysis of biologically active endogenous carboxylic acids

Author

Kloos, D., Lingeman, H., Mayboroda, O.A., Deelder, A.M., Niessen, W.M.A., Giera, M., BioAnalytical Chemistry, Molecular Cell Physiology, and AIMMS

Abstract

Carboxylic acids (CAs), such as small CAs, fatty acids, eicosanoids and bile acids, are involved in numerous biological processes. Mapping the participating pathways potentially yields great insight into the physiological state of an organism. There is demand for analytical techniques that are more sensitive, faster and easier to handle. These would enable advanced analysis and validation in larger clinical cohorts and hopefully deliver useful disease markers. The analysis of CAs is not only driven by the CA group, but also largely dependent on chain length and other functional groups present. Several liquid and gas chromatography strategies, with or without derivatization, were developed in recent years. Here, we review the most recent trends in analysis of endogenous CAs by chromatography-mass spectrometry. We critically evaluate sample preparation, derivatization techniques, separation and mass spectrometric detection. Ultimately, the reader is guided to the most versatile, sensitive and easy analytical methods.

Published
2014
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48. Comprehensive GC–MS analysis of fatty acids and sterols using sequential one-pot silylation: quantification and isotopologue analysis

Author

Kloos, D., Gay, E, Lingeman, H., Bracher, F., Müller, C., Mayboroda, O.A., Deelder, A.M., Niessen, W.M.A., Giera, M., BioAnalytical Chemistry, Molecular Cell Physiology, and AIMMS

Subjects
SDG 6 - Clean Water and Sanitation
Abstract

RATIONALEFatty acids and sterol lipids play crucial roles in several biological processes and several biological facts underline the interconnection between these lipid classes. Therefore, it is of interest to develop a comprehensive method analysing both classes in the form of their most favourable derivatives suitable for quantification and isotopologue analysis. METHODSLipids were derivatised by a sequential one-pot procedure using N-tert-butyldimethylsilyl-N-methyltrifluoroacetamide (MtBSTFA) and N,O-bis(trimethylsilyl)trifluoroacetamide (BSTFA). No clean-up or concentration steps were necessary. The prepared samples were directly available for gas chromatography-electron ionisation mass spectrometric (GC-EI-MS) analysis on a standard column. For quantification, the SIM mode was used and for isotopologue analysis scheduled scan mode was applied. RESULTSDevelopment of a sequential one-pot derivatisation for GC-EI-MS allowing comprehensive analysis of fatty acids and sterols as their most favourable derivatives. Validation carried out using human plasma, comparison with certified NIST plasma. LLOQ of usually 3.3 ng/mL achieved. Isotopologue analysis of 2-[

Published
2014
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49. Abstracts of lectures symposium disposition and delivery of peptide drugs

Author

van Nispen, J. W., Hichens, M., Sauter, A., Lingeman, H., Cubbins, D. C., McMartin, C., Webb, R. L., Wennogle, L. P., Wysowskyi, H. E., Zimmerman, M. B., Lee, V. H. L., Sandow, J., Seidel, H., Schmiedel, R., Keller, Bradley T., Smith, Kevin R., Borchardt, Ronald T., Banks, W. A., Kastin, A. J., de Wied, D., DeLuca, P. P., Robinson, J. R., Lundin, S., Vilhardt, H., Saffran, M., Kumar, G. S., Neckers, D. G., Williams, F., Field, J. B., Jones, R. H., Panepinto, L., Harris, A. S., Moses, Alan C., Muranishi, S., Boddé, H. E., Ponec, M., Verhoef, J., Liversidge, Gary G., Boer, G. J., Kruisbrink, J., de Nijs, H., Bouwman, T. R. M., Eenink, M. J. D., and Patel, Harish M.

Published
1988
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50. Abstracts of papers

Author

van Oort, W. J., Kerkhofs, B., van Dijk, A., van der Houwen, O. A. G. J., Hulshoff, A., Indemans, A. W. M., Reijenga, J. C., Gaykema, A., Mikkers, F. E. P., Leeuwenkamp, O. R., Jousma, H., van der Mark, E. J., Bult, A., van Iersel, W., Drenth, B. F. H., Ghijsen, R. T., de Zeeuw, R. A., Holthuis, J. J. M., Sijstermans, A. W., Römkens, F. M. G. M., Weller, E. B. C. M., Pinedo, H. M., McVie, J. G., Barends, P. M., Smits, M. H., Blauw, J. S., den Hartigh, J., Driebergen, R. J., Schijns, J. E. M. A., Underberg, W. J. M., Lake, O. A., Lingeman, H., Underberg-Chitoe, U. K., Wilting, J., Jagersma, T., Hoogvliet, J. C., Elferink, F., Hermans-Lokkerbol, A. C. J., van Bennekom, W. P., Werkhoven-Goewie, C. E., de Ruiter, C., Brinkman, U. A. Th., Frei, R. W., de Vries, G., van de Calseyde, J. F., van der Veeken, J., Verheggen, Th. P. E. M., Everaerts, F. M., van der Vijgh, W. J. F., van der Lee, H. B. J., Postma, G. J., Vree, Tom B., Hekster, Chiel A., Oosterbaan, Marijn M. J., Termond, Emiel F. S., Schoots, A. C., Cramers, C. A., Poppe, H., van de Vaart, F. J., Claessens, H. A., van Thiel, M., Westra, P., Labout, J. J. M., Bruins, A. P., and Drenth, B. F. H.

Published
1982
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