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4:00 pm Tuesday, February 3 Proteomics – Arrays Room B1<br />

Zheng Ouyang<br />

Purdue University<br />

560 Oval Drive<br />

West Lafayette, Indiana 47906<br />

ouyang@purdue.edu<br />

Protein Array Preparation by Ion Soft-L<strong>and</strong>ing<br />

83<br />

Co-Author(s)<br />

Z. Takats, T. M. Blake,<br />

B. Gologan, J. M. Wiseman,<br />

J. C. Oliver, V. J. Davisson,<br />

R. G. Cooks<br />

A new method has been developed <strong>for</strong> preparing microarrays of biomolecules via soft-l<strong>and</strong>ing of mass selected,<br />

multiply-changed ions. A modified single quadrupole mass filter <strong>and</strong> a custom-built linear ion trap mass<br />

spectrometer have been used to select the ions <strong>and</strong> deposit them onto surfaces including: polycrystalline gold,<br />

functionalized self-assembled monolayers, <strong>and</strong> liquid thin films, at l<strong>and</strong>ing energies of 10-20 eV. The effectiveness<br />

of this method has been demonstrated via the preparation of a four-component array of proteins from a mixture<br />

of cytochrome C, apomyoglobin, lysozyme <strong>and</strong> insulin. The l<strong>and</strong>ed materials were recovered <strong>and</strong> analyzed by<br />

electrospray <strong>and</strong> MALDI mass spectrometry as well as being characterized in situ by laser desorption. Biological<br />

activity of the l<strong>and</strong>ed species was confirmed in the case of lysozyme, <strong>and</strong> in other experiments in the cases of<br />

trypsin, hexokinase <strong>and</strong> protein kinase A. The l<strong>and</strong>ing efficiencies were estimated to be a few tens of % <strong>and</strong><br />

the spot sizes are ca. 1 mm in radius. The conditions <strong>for</strong> the soft-l<strong>and</strong>ing of proteins <strong>and</strong> peptides have been<br />

optimized. Neutralization of the ions on the surfaces was studied <strong>and</strong> both complete <strong>and</strong> incomplete neutralization<br />

were found, depending on the properties of the surfaces. The applications of this method to biology study <strong>and</strong><br />

drug discovery as well as the modification of commercial mass spectrometers <strong>for</strong> soft-l<strong>and</strong>ing are discussed.<br />

4:30 pm Tuesday, February 3 Proteomics – Arrays Room B1<br />

Peter Wagner<br />

Zyomyx, Inc.<br />

26101 Research Road<br />

Hayward, Cali<strong>for</strong>nia 94545<br />

pwagner@zyomyx.com<br />

New Detection Principles <strong>for</strong> Protein Biochips<br />

Protein biochips are becoming increasingly important <strong>for</strong> extracting comprehensive biological in<strong>for</strong>mation<br />

from smallest sample volumes. Applications include the quantification of gene expression at the protein level,<br />

the measurement of protein-protein interactions, as well as functional protein activity. The diversity in protein<br />

measurements <strong>and</strong> assay variations requires different types of chip architectures <strong>and</strong> detection modes. Zyomyx is<br />

uniquely positioned to address the problems associated with micro-scale protein detection <strong>and</strong> characterization.<br />

Using proprietary biochip-based tools, Zyomyx has developed several novel plat<strong>for</strong>ms <strong>for</strong> proteomic research. An<br />

overview of protein biochip technologies will be presented with an emphasis on label-independent detection.<br />

PODIUM ABSTRACTS

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