Optimization of Matrix Conditions for the Control of MALDI In-Source Decay of Permethylated Glycans.

Smargiasso, Nicolas; De Pauw, Edwin

doi:10.1021/ac1017452

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Optimization of Matrix Conditions for the Control of MALDI In-Source Decay of Permethylated Glycans.

Smargiasso, Nicolas; De Pauw, Edwin

2010 • In Analytical Chemistry, sous presee

Peer Reviewed verified by ORBi

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https://hdl.handle.net/2268/74800

DOI
10.1021/ac1017452

PubMed
21028830

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Keywords :

Mass Spectrometry; Glycans; MALDI-ISD; MALDI IMAGING

Abstract :

[en] Due to its fastness and its easiness to use, MALDI-MS is currently an analytical tool widely used in glycomic applications. However, the MALDI ionization process could result in the so-called "in-source decay", or ISD, of analytes, leading to complex spectra. On the other hand, ISD opens the possibility to perform pseudo-MS(3) experiments. This phenomenon must therefore be controlled in order to be used on demand as a supplementary tool for the analysis of permethylated glycans by MALDI mass spectrometry. For this purpose, several matrices were tested and MALDI imaging was used to determine optimal conditions promoting or, inversely, avoiding ISD of permethylated glycans. 2,5-DHB was shown to be a versatile matrix allowing one to induce or prevent ISD according to the location of laser shots. Inversely, it was shown that 9-aminoacridine forms homogeneous spots and avoids completely ISD. This matrix would therefore be suitable for automatic analysis.

Research Center/Unit :

Giga-Systems Biology and Chemical Biology - ULiège
CART - Centre Interfacultaire d'Analyse des Résidus en Traces - ULiège

Disciplines :

Chemistry
Biochemistry, biophysics & molecular biology

Author, co-author :

Smargiasso, Nicolas ; Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.)

De Pauw, Edwin ; Université de Liège - ULiège > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.)

Language :

English

Title :

Optimization of Matrix Conditions for the Control of MALDI In-Source Decay of Permethylated Glycans.

Publication date :

2010

Journal title :

Analytical Chemistry

ISSN :

0003-2700

eISSN :

1520-6882

Publisher :

American Chemical Society, Washington, United States - District of Columbia

Volume :

sous presee

Peer reviewed :

Peer Reviewed verified by ORBi

Additional URL :

http://pubs.acs.org/doi/abs/10.1021/ac1016198

Name of the research project :

GLYCO (FEDER)

Funders :

FEDER - Fonds Européen de Développement Régional
F.R.S.-FNRS - Fonds de la Recherche Scientifique

Available on ORBi :

since 01 November 2010

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Bibliography

Morelle, W. and Michalski, J. C. Nat. Protoc. 2007, 2, 1585-1602
Harvey, D. J. Int. J. Mass Spectrom. 2003, 226, 1-35
Zaia, J. Chem. Biol. 2008, 15, 881-892
Bigge, J. C., Patel, T. P., Bruce, J. A., Goulding, P. N., Charles, S. M., and Parekh, R. B. Anal. Biochem. 1995, 230, 229-238
North, S. J., Hitchen, P. G., Haslam, S. M., and Dell, A. Curr. Opin. Struct. Biol. 2009, 19, 498-506
Brown, R. S. and Lennon, J. J. Anal. Chem. 1995, 67, 3990-3999
Takayama, M. J. Am. Soc. Mass Spectrom. 2001, 12, 420-427
Sakakura, M. and Takayama, M. J. Am. Soc. Mass Spectrom. 2010, 21, 979-988
Demeure, K., Quinton, L., Gabelica, V., and De Pauw, E. Anal. Chem. 2007, 79, 8678-8685
Wang, B. H., Hopkins, C. E., Belenky, A. B., and Cohen, A. S. Int. J. Mass Spectrom. 1997, 169, 331-350
Yamagaki, T. and Nakanishi, H. J. Mass Spectrom. 2000, 35, 1300-1307
Harvey, D. J. Proteomics 2001, 1, 311-328
Bashir, S., Giannakopulos, A. E., Derrick, P. J., Critchley, P., Bottrill, A., and Padley, H. J. Eur. J. Mass Spectrom. 2004, 10, 109-120
Kameyama, A., Kaneda, Y., Yamanaka, H., Yoshimine, H., Narimatsu, H., and Shinohara, Y. Anal. Chem. 2004, 76, 4537-4542
Yamagaki, T., Suzuki, H., and Tachibana, K. J. Am. Soc. Mass Spectrom. 2006, 17, 67-74
Yamagaki, T., Suzuki, H., and Tachibana, K. Anal. Chem. 2005, 77, 1701-1707
Lennon, J. J. and Walsh, K. A. Protein Sci. 1999, 8, 2487-2493
Suckau, D. and Resemann, A. Anal. Chem. 2003, 75, 5817-5824
Quinton, L., Demeure, K., Dobson, R., Gilles, N., Gabelica, V., and De Pauw, E. J Proteome Res. 2007, 6, 3216-3223
Resemann, A., Wunderlich, D., Rothbauer, U., Warscheid, B., Leonhardt, H., Fuchser, J., Kuhlmann, K., and Suckau, D. Anal. Chem. 2010, 82, 3283-3292
Takayama, M. and Tsugita, A. Electrophoresis 2000, 21, 1670-1677
Debois, D., Bertrand, V., Quinton, L., De Pauw-Gillet, M. C., and De Pauw, E. Anal. Chem. 2010, 82, 4036-4045
Domon, B. and Costello, C. E. Glycoconjugate J. 1988, 5, 397-409
Suzuki, N., Khoo, K. H., Chen, C. M., Chen, H. C., and Lee, Y. C. J. Biol. Chem. 2003, 278, 46293-46306
Yu, S. Y., Khoo, K. H., Yang, Z., Herp, A., and Wu, A. M. Glycoconjugate J. 2008, 25, 199-212
Yu, S. Y., Wu, S. W., and Khoo, K. H. Glycoconjugate J. 2006, 23, 355-369
Terada, M., Khoo, K. H., Inoue, R., Chen, C. I., Yamada, K., Sakaguchi, H., Kadowaki, N., Ma, B. Y., Oka, S., Kawasaki, T., and Kawasaki, N. J. Biol. Chem. 2005, 280, 10897-10913
Klisch, K., Jeanrond, E., Pang, P. C., Pich, A., Schuler, G., Dantzer, V., Kowalewski, M. P., and Dell, A. Glycobiology 2008, 18, 42-52
Wuhrer, M. and Deelder, A. M. Rapid Commun. Mass Spectrom. 2006, 20, 943-951
Dell, A., Reason, A. J., Khoo, K. H., Panico, M., McDowell, R. A., and Morris, H. R. Methods Enzymol. 1994, 230, 108-132
Dell, A., Jang-Lee, J., Pang, P.-C., Parry, S., Sutton-Smith, M., Tissot, B., Morris, H. R., Panico, M., and Haslam, S. M. Eds.; Glycoscience; Springer-Verlag: New York, 2008.
Hanton, S. D., Clark, P. A. C., and Owens, K. G. J. Am. Soc. Mass Spectrom. 1999, 10, 104-111
Garden, R. W. and Sweedler, J. V. Anal. Chem. 2000, 72, 30-36
Luxembourg, S. L., McDonnell, L. A., Duursma, M. C., Guo, X., and Heeren, R. M. Anal. Chem. 2003, 75, 2333-2341
Vermillion-Salsbury, R. L. and Hercules, D. M. Rapid Commun. Mass Spectrom. 2002, 16, 1575-1581
Dannenberger, D., Suss, R., Teuber, K., Fuchs, B., Nuernberg, K., and Schiller, J. Chem. Phys. Lipids 2010, 163, 157-164
Armstrong, D. W., Zhang, L. K., He, L., and Gross, M. L. Anal. Chem. 2001, 73, 3679-3686
Tholey, A. and Heinzle, E. Anal. Bioanal. Chem. 2006, 386, 24-37
Mank, M., Stahl, B., and Boehm, G. Anal. Chem. 2004, 76, 2938-2950
Laremore, T. N., Murugesan, S., Park, T. J., Avci, F. Y., Zagorevski, D. V., and Linhardt, R. J. Anal. Chem. 2006, 78, 1774-1779
Bungert, D., Bastian, S., Heckmann-Pohl, D. M., Giffhorn, F., Heinzle, E., and Tholey, A. Biotechnol. Lett. 2004, 26, 1025-1030
Guillard, M., Gloerich, J., Wessels, H. J., Morava, E., Wevers, R. A., and Lefeber, D. J. Carbohydr. Res. 2009, 344, 1550-1557
Dogruel, D., Nelson, R. W., and Williams, P. Rapid Commun. Mass Spectrom. 1996, 10, 801-804
Tzeng, Y. K., Chang, C. C., Huang, C. N., Wu, C. C., Han, C. C., and Chang, H. C. Anal. Chem. 2008, 80, 6809-6814
Sheeley, D. M., Merrill, B. M., and Taylor, L. C. Anal. Biochem. 1997, 247, 102-110
Patel, T. P., Parekh, R. B., Moellering, B. J., and Prior, C. P. Biochem. J. 1992, 285 (3) 839-845