Laser-assisted protein adsorption

This proposal describes the development of a new, systematic approach for qualitatively and quantitatively studying surface-biomolecule interactions by matrix-assisted laser desorption ionization (MALDl) mass spectrometry (MS). This methodology is being developed because of the profound importance that surface-biomolecule interactions play in applications where biomaterials come into contact with complex biological fluids, it can readily be shown that undesired reactions occurring in response to surface-biomolecule contact (protein adsorption, biofouling, immune response activation, etc.) lead to enormous economic and human costs. Thus, the development of analytical methodologies that allow for efficient assessment of the properties of new biomaterials and/or the study of detailed fundamental processes initiated upon surface-biomolecule contact are of critical value ... 

Belisle, J. M., Correia, J. P., Wiseman, P. W., Kennedy, T. E., Costantino, S. (2008). Patterning protein concentration using laser-assisted adsorption by photobleaching, LAPAP. Lab on a Chip, 8 2), 2164. 

Pfleging, W, Torge, M., Bruns, M., Troudlet, V., Welle, A., and Wilson, S. (2009) Laser- and UV-assisted modification of polystyrene surfaces for control of protein adsorption and cell adhesion. Appl. Surf. Sci., 255, 5453-5457. 

Matrix-assisted laser desertion ionization (MALDI) was first described by Karas and Hillenkamp in 1988 [469]. At that time it was a revolutionary method for the ionisation and analysis of large biomolecules. Now many more MS methods have been devised, but the analysis of complete protein masses is still only possible by MALDI [470]. With MALDI, a matrix (crystals of small organic molecules) with a small amount of analyte is ionised by a short laser pulse at a wavelength close to the adsorption band of the matrix molecules. This produces predominantly singly charged molecular ions, which are detected by the TOE spectrometer. The ana-... 

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