AVS 51st International Symposium
    Biomaterial Interfaces Monday Sessions
       Session BI-MoP

Paper BI-MoP8
Surface Modified MALDI Probes for Affinity Fractionation of Protein Mixtures

Monday, November 15, 2004, 5:00 pm, Room Exhibit Hall B

Session: Poster Session
Presenter: M. Li, University of Texas at Arlington
Authors: G.R. Kinsel, University of Texas at Arlington
M. Li, University of Texas at Arlington
G. Fernando, University of Texas at Arlington
L. van Waasbergen, 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 separation and purification of peptides/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 peptide and protein separation based on their hydrophobicity. Pulsed RF plasma deposition of allyl alcohol directly on the MALDI probe surface is used to produce surfaces with various hydrophobicities. Control of the degree of the hydrophobicity is achieved through changes in the duty cycle of the pulsed RF plasma. Testing of the surfaces for peptide/protein separation based on their hydrophobicity is performed using various laboratory prepared control mixtures and mixtures obtained from biological sources. In all cases fractionation of the protein/peptide mixture was evaluated through the acquisition MALDI mass spectra using a Bruker AutoFLEX MALDI TOFMS or a laboratory-constructed linear MALDI TOFMS. Data has been obtained from surfaces with different hydrophobicities that demonstrate the efficacy of these modified MALDI probe surfaces for achieving on-probe fractionation of peptide/protein mixtures.