AVS 50th International Symposium
    Biomaterial Interfaces Friday Sessions
       Session BI+PS-FrM

Paper BI+PS-FrM4
Combining Pulsed RF Plasma Polymer Coatings with Avidin-Biotin Chemistry for On-Probe Affinity Capture Mass Spectrometry

Friday, November 7, 2003, 9:20 am, Room 318/319

Session: Plasma Methods for Bio-interfaces
Presenter: G.R. Kinsel, University of Texas at Arlington
Authors: G.R. Kinsel, University of Texas at Arlington
M. Li, University of Texas at Arlington
R.B. Timmons, University of Texas at Arlington
Correspondent: Click to Email
Matrix assisted laser desorption / ionization mass spectrometry (MALDI-MS) has become a powerful analytical tool for the characterization of proteins. As the effectiveness of the MALDI method has advanced, the need for high-speed isolation and purification of targeted proteins in complex mixtures (e.g. culture media, serum or urine) has increased. The approach described in this presentation focuses on the use of RF plasma polymer coated MALDI probes as platforms for introduction of avidin/biotin chemical modifications. Pulsed RF plasma deposition of allyl amine or vinyl carboxylic acid directly on the MALDI probe surface is used to produce amine modified and carboxylic acid modified surfaces, respectively. Control of the functional group density is achieved through changes in the duty cycle of the pulsed RF plasma. Both amine and carboxylic acid functionalized plasma polymer modified probe surfaces have been investigated as platforms for attachment of avidin or biotin. Testing of the surfaces for peptide/protein isolation based on the targeted properties is performed using various laboratory prepared control mixtures and mixtures obtained from biological sources. In all cases selective capture of the targeted protein/peptide was evaluated through the acquisition MALDI mass spectra using a Bruker BiFLEX linear MALDI TOFMS or a laboratory-constructed linear MALDI TOFMS. Data has been obtained from both avidin and biotin surfaces demonstrating the efficacy of these modified MALDI probe surfaces for achieving on-probe bioselective isolation of target compounds.