Top-Down Mass Spectrometry Imaging of Intact Proteins by LAESI FT-ICR MS

Laser Ablation Electrospray Ionization is a recent development in mass spectrometry imaging. It has been shown that lipids and small metabolites can be imaged in various samples such as plant material, tissue sections or bacterial colonies without anysample pre-treatment. Further, laser ablation ele...

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Bibliographic Details
Published inarXiv.org
Main Authors Kiss, András, Smith, Donald F, Reschke, Brent R, Powell, Matthew J, Heeren, Ron M A
Format Paper
LanguageEnglish
Published Ithaca Cornell University Library, arXiv.org 04.09.2013
Subjects
Ablative materials
Dissociation
Electrospraying
Fragmentation
Hemoglobin
Imaging
Infrared lasers
Ion sources
Ionization
Ions
Laser ablation
Lipids
Mass spectrometry
Metabolites
Pretreatment
Proteins
Proteomics
Scientific imaging
Solid surfaces
Spectroscopy
Tissues
Viability
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Summary:Laser Ablation Electrospray Ionization is a recent development in mass spectrometry imaging. It has been shown that lipids and small metabolites can be imaged in various samples such as plant material, tissue sections or bacterial colonies without anysample pre-treatment. Further, laser ablation electrospray ionization has been shown to produce multiply charged protein ions from liquids or solid surfaces. This presents a means to address one of the biggest challenges in mass spectrometry imaging; the identification of proteins directly from biological tissue surfaces. Such identification is hindered by the lack of multiply charged proteins in common MALDI ion sources and the difficulty of performing tandem MS on such large, singly charged ions. We present here top-down identification of intact proteins from tissue with a LAESI ion source combined with a hybrid ion-trap FT-ICR mass spectrometer. The performance of the system was first tested with a standard protein with ECD and IRMPD fragmentation to prove the viability of LAESI FT-ICR for top-down proteomics. Finally, the imaging of a tissue section was performed, where a number of intact proteins were measured and the hemoglobin {\alpha} chain was identified directly from tissue using collision-induced dissociation and infrared multiphoton dissociation fragmentation.
ISSN:2331-8422