AVS 49th International Symposium
    Biomaterials Tuesday Sessions
       Session BI+SS-TuM

Paper BI+SS-TuM5
Characterization of Non-Fouling Surfaces by Matrix-Assisted Laser Desorption / Ionization Mass Spectrometry

Tuesday, November 5, 2002, 9:40 am, Room C-201

Session: Platforms for Non-fouling and Patterned Surfaces
Presenter: G.R. Kinsel, University of Texas at Arlington
Authors: G.R. Kinsel, University of Texas at Arlington
J. Zhang, University of Texas at Arlington
R.B. Timmons, University of Texas at Arlington
M. Li, University of Texas at Arlington
Correspondent: Click to Email
Matrix-Assisted Laser Desorption / Ionization (MALDI) mass spectrometry has emerged in recent years as a powerful method for the mass spectrometric analysis of a wide range of biomolecules including proteins, oligonucleotides, polysaccharides, etc. An attractive feature of this analytical approach is the relative simplicity of the sample preparation. In principle, all that is required is that the analyte of interest be mixed with an appropriate "matrix" (typically a small, functionalized aromatic compound) and the two compounds allowed to co-crystallize on some type of support. In recent work, however, we have shown that the nature of the support can have a marked effect on the magnitude of the analyte MALDI ion signal. Specifically, we have shown that as the binding affinity of the support for the analyte increases, the analyte MALDI ion signal decreases. This relationship has been used to develop a quantitative method for the determination of the protein binding affinity of various materials based on a MALDI standard additions approach. In the present studies the MALDI method has been used to quantitate the protein binding affinity of a number of "non-fouling" surfaces. These surfaces include plasma polymerized PEO, plasma polymerized CH3OH, PEO-PU block copolymers, and PEO grafted surfaces. The "non-fouling" properties of these surfaces are compared with the protein binding affinity of other conventional polymers including PTFE, LDPE, etc. In addition, the binding properties of the various surfaces are examined with relation to a variety of peptides and modest sized proteins.