AVS 52nd International Symposium
    Biomaterial Interfaces Friday Sessions
       Session BI+SS-FrM

Paper BI+SS-FrM5
Characterisation of Analyte / Matrix Interaction for MALDI / TOF Targets Using Spatially Resolved X-ray Photoelectron Spectroscopy

Friday, November 4, 2005, 9:40 am, Room 311

Session: Biomaterials Surface Characterization
Presenter: A.J. Roberts, Kratos Analytical Ltd, UK
Authors: A.J. Roberts, Kratos Analytical Ltd, UK
D.J. Surman, Kratos Analytical Ltd, UK
S.J. Hutton, Kratos Analytical Ltd, UK
M. Resch, SDG, Germany
E. Raptakis, Kratos Analytical Ltd, UK
O. Belgacem, Kratos Analytical Ltd, UK
Correspondent: Click to Email
Matrix-assisted laser desorption/ionisation (MALDI) is now an established technique for mass spectrometry of proteins and peptides. Different matrix-analyte preparation protocols have been shown to influence the desorption or ablation process resulting in either high or low metastable fragmentation. It has been speculated that following laser ablation the velocities of the analyte and matrix can be regarded as a valuable and meaningful characteristic of the MALDI process. However, the interaction and distribution of the analyte with respect to the matrix is poorly understood. Here we present a study of the distribution of a fluorinated peptide as a function of matrix material using imaging x-ray photoelectron spectroscopy (XPS). Both the lateral and depth distribution is investigated to draw conclusions on the incorporation of the analyte in the matrix.