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Article

Attomole Peptide Analysis by High-Pressure Matrix-Assisted Laser Desorption/Ionization Fourier Transform Mass Spectrometry

Susanne C. Moyer,^† Bogdan A. Budnik,^‡ Jason L. Pittman,^† Catherine E. Costello,^†^‡ and Peter B. O'Connor*^†^‡

Mass Spectrometry Resource and Cardiovascular Proteomics Center, Boston University School of Medicine, 715 Albany Street, Boston, Massachusetts 02118-2526

Anal. Chem., 2003, 75 (23), pp 6449–6454

DOI: 10.1021/ac034938x

Publication Date (Web): October 31, 2003

†

Mass Spectrometry Resource.

‡

Cardiovascular Proteomics Center.

Corresponding author. Phone: (617) 638-6705. Fax: (617) 638-6761. E-mail: poconnor@bu.edu.

Abstract

A new high-pressure matrix-assisted laser desorption/ionization (HP-MALDI) source for FTMS has recently been described (O'Connor et al. J. Am. Soc. Mass Spectrom., in press). Improvements to the source design, including the incorporation of a new high-pressure gas channel plate, resulted in ions devoid of metastable fragmentation and also in increased sensitivity compared to the HP-MALDI prototype source design. The focus of this contribution is the evaluation of the current HP-MALDI FTMS configuration. The use of nonconductive sample surfaces, such as Parafilm and Teflon, was explored, and spectra from 30 amol of peptide applied to these surfaces were routinely obtained. In addition, the current limit of detection for this configuration is demonstrated to be 300 zmol for the phosphopeptide RRREEE(pS)EEEAA using multishot accumulation of the ions from 15 laser shots in the hexapole and 1 scan. In addition, the performance of the new HP-MALDI FTMS configuration and its potential application for high-throughput proteomics analyses are discussed.

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