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Published Online August 14, 2003
Science DOI: 10.1126/science.1088776

Reports

Submitted on July 3, 2003
Accepted on August 5, 2003

Preparing Protein Microarrays by Soft Landing of Mass-Selected Ions

Zheng Ouyang 1, Zoltán Takáts 1, Thomas A. Blake 1, Bogdan Gologan 1, Andy J. Guymon 1, Justin M. Wiseman 1, Justin C. Oliver 2, V. Jo Davisson 2, R. Graham Cooks 1*

1 Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
2 Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.

* To whom correspondence should be addressed. E-mail: cooks{at}purdue.edu.

Intact, multiply protonated proteins of particular mass and charge are selected from ionized protein mixtures and gently landed at different positions on a surface to form a microarray. An array of cytochrome c, lysozyme, insulin, and apomyoglobin was generated, and the deposited proteins showed electrospray ionization mass spectra that matched those of the authentic compounds. Deposited lysozyme and trypsin retained their biological activity. Multiply charged ions of protein kinase A catalytic subunit and hexokinase were also soft landed into glycerol-based liquid surfaces. These soft-landed kinases phosphorylated LRRASLG oligopeptide and D-fructose, respectively.





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Science. ISSN 0036-8075 (print), 1095-9203 (online)