Reference : MALDI-In Source Decay Applied to Mass Spectrometry Imaging: A New Tool for Protein Id...
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 mailto [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
Bertrand, Virginie mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie - Cytologie >]
Quinton, Loïc mailto [Université de Liège - ULg > Département de chimie (sciences) > GIGA-R : Laboratoire de spectrométrie de masse (L.S.M.) >]
De Pauw, Marie-Claire mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Histologie - Cytologie - Département des sciences biomédicales et précliniques >]
De Pauw, Edwin mailto [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
Yes (verified by ORBi)
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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