| Reference : MALDI-In Source Decay Applied to Mass Spectrometry Imaging: A New Tool for Protein Ident... |
| Scientific journals : Article | |||
| Human health sciences : Multidisciplinary, general & others Physical, chemical, mathematical & earth Sciences : Chemistry Life sciences : Biochemistry, biophysics & molecular biology | |||
| http://hdl.handle.net/2268/13543 | |||
| MALDI-In Source Decay Applied to Mass Spectrometry Imaging: A New Tool for Protein Identification. | |
| English | |
Debois, Delphine [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >] | |
Bertrand, Virginie [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie - Cytologie >] | |
Quinton, Loïc [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >] | |
De Pauw, Marie-Claire [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie - Cytologie - Département des sciences biomédicales et précliniques >] | |
De Pauw, Edwin [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >] | |
| 15-May-2010 | |
| Analytical Chemistry | |
| American Chemical Society | |
| 82 | |
| 10 | |
| 3969-4304 | |
| International | |
| 0003-2700 | |
| 1520-6882 | |
| Washington | |
| DC | |
| [en] Mass Spectrometry ; MALDI imaging ; Top-down proteomics | |
| [en] Matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) imaging is a powerful technique giving access to the distribution of a large range of biomolecules directly from a tissue section, allowing, for example, the discovery of new pathological biomarkers. Nevertheless, one main difficulty lies in the identification of the detected species, especially proteins. MALDI-in source decay (ISD) is used to fragment ions directly in the mass spectrometer ion source. This technique does not require any special sample treatment but only the use of a specific MALDI matrix such as 2,5-dihydroxybenzoic acid or 1,5-diaminonaphthalene. MALDI-ISD is generally employed on classical, purified samples, but here we demonstrate that ISD can also be performed directly on mixtures and on a tissue slice leading to fragment ions, allowing the identification of major proteins without any further treatment. On a porcine eye lens slice, de novo sequencing was even performed. Crystallins not yet referenced in databases were identified by sequence homology with other mammalian species. On a mouse brain slice, we demonstrate that results obtained with ISD are comparable and even better than those obtained with a classical in situ digestion. | |
| Giga-Systems Biology and Chemical Biology ; Centre Interfacultaire d'Analyse des Résidus en Traces - CART | |
| Fonds Européen de Développement Régional - FEDER ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Région wallonne : Direction générale des Technologies, de la Recherche et de l'Energie - DGTRE | |
| Researchers ; Professionals ; Students | |
| http://hdl.handle.net/2268/13543 | |
| 10.1021/ac902875q |
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