April 2003 Meeting Announcement, Delaware Valley Mass Spectrometry Discussion Group
- Topic: "Pulsed Plasma Polymer Modified Surfaces for Bio-Selective MALDI Probe Preparation "
- Speaker:Gary Kinsel
- Date: Monday, April 14, 2003. 6:30 PM
- Time: Social Hour: 6:30 PM. (Pizza and Beer)
Talk: 7:30 PM.
- Place: Widener University, University Center, Webb Room.
- Abstract: Recent work in our laboratory has focused on the development of MALDI probes having surfaces tailored to allow affinity capture of targeted peptides and proteins, either through biospecific or class-specific interactions. These surfaces have been produced by pulsed RF plasma deposition of various monomers directly onto the MALDI probe. This approach allows both control of the surface chemical functionality and functional group density through changes in the monomer used for plasma polymerization and the duty cycle of the pulsed RF plasma. Amine and carboxylic acid functionalized probe surfaces have been used to synthesize biotin-modified surfaces and demonstrated to selectively capture avidin from avidin containing mixtures of proteins. In their unmodified form these same surfaces have also been used to selectively isolate peptides from mixtures on the basis of peptide pI. This approach has been shown to allow cirumvention of the MALDI ion suppression effect in which basic peptides tend to reduce the MALDI signal intensity of co-mixed acidic peptides. Copper impregnated carboxylic modified surfaces have been shown to allow the selective on-probe isolation of phosphopeptides while hydrophobic surfaces, produced by pulsed RF plasma deposition of allyl alcohol, have been shown to allow the separation of peptide mixtures on the basis of hydrophobicity. Finally, ethylene oxide modified surfaces, originally developed for use as non-fouling coatings of biomaterials (e.g. contact lenses) have been shown to allow substantial reductions in the limits of detection for various peptides and proteins. Cumulatively, these studies demonstrate how large-scale improvements in MALDI analysis can be achieved through intelligent design of MALDI probe surface chemistry and suggest that this approach should hold particular value for MALDI based high-throughput screening applications.
- Bio: Gary Kinsel is an associate professor of analytical chemistry at the University of Texas at Arlington. He has a BS in Chemistry from Western Illinois University and completed his PhD with Murray Johnston at the University of Colorado. He was a Post Doctoral Fellow at the Technical University of Munich on an Alexander von Humboldt Research Fellowship and at Texas A&M with David Russell. He has extensive experience in analytical chemistry with broad experience in most modern analytical techniques and specific expertise in mass spectrometry, scanning probe microscopy and laser spectroscopy. This includes; resonant 2-photon ionization (R2PI) mass spectrometry, custom mass spectrometer instrument design, supersonic jet expansions for laser spectroscopy and laser ionization mass spectrometry, tunable laser ionization characterization of cluster species, Matrix Assisted Laser Desorption / Ionization mass spectrometry, conventional bioanalytical techniques including proteolytic digestion, gel separation, etc., surface characterization techniques including XPS, goniometry, AFM and FTIR spectroscopy, thin film coatings for surface preparation via RF pulsed plasma polymer formation. He has received the Outstanding Teacher of the Year Award from the University of Texas at Arlington, College of Science and the National Science Foundation CAREER Award for Analytical Applications of MALDI Mass Spectrometry to the Study of Surface-Protein interactions.
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