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High Resolution Fourier Transform-ICR Biopolymer Mass Spectrometry: New Approaches in Proteome Analysis, Characterisation of Complex Biological Mixtures and Combinatorial ChemistryThe development of efficient "soft ionisation" methods in the last years has
provided the basis for the molecular characterisation of biopolymers by mass
spectrometry. In contrast to previous limitations in the molecular weight range
amenable, electrospray ionisation (ESI-MS) and matrix assisted laser desorption
ionisation (MALDI-MS) have provided access to biopolymers >> 100 kDa. The recent
development of Fourier transform ion cyclotron resonance (FTICR) mass
spectrometry enabled a breakthrough for the ultra-high resolution mass
spectrometric analysis of biopolymers using both ESI and MALDI ionisation (A.G.
Marshall, Mass Spectrom. Rev. 17, 1, 1998). Present studies in our laboratory on
the analytical development of ESI-FTICR mass spectrometry focus on (i) the
structure analysis of non-covalent supramolecular biopolymer complexes; (ii) the
direct, high resolution mass spectrometry of peptide mixtures in proteome
analysis and analysis of combinatorial mixtures; and (iii) the identification of
antigen determinant structures of mono- and polyclonal antibodies using the mass
spectrometric epitope mapping method developed in our laboratory (M. Przybylski,
Adv. Mass Spectrom. 13, 275, 1995). For this new interdisciplinary DFG research
programme, a 7 T Bruker FTICR MS instrument with Apollo electrospray and nano
electrospray ionisation sources, micro LC-MS and CE-MS facilities, a new
MALDI-MS ionisation source with IR-MPD equipment has been installed. New
biochemical applications of FTICR-MS are the structure elucidation of cell
surface proteins, the epitope elucidation of target antigens in auto-immune
diseases and the characterisation of cell-specific proteins for apoptosis. In
these studies FTICR-MS is providing new analytical perspectives to biochemical
and cell-biological applications of biopolymer structure analysis. |
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