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On-probe solid-phase extraction/MALDI-MS using ion-pairing interactions for the cleanup of peptides and proteins.

Authors
  • Warren, M E
  • Brockman, A H
  • Orlando, R
Type
Published Article
Journal
Analytical chemistry
Publication Date
Sep 15, 1998
Volume
70
Issue
18
Pages
3757–3761
Identifiers
PMID: 9751020
Source
Medline
License
Unknown

Abstract

Samples originating from biological sources often contain a complex mixture of inorganic salts, buffers, chaotropic agents, surfactants/detergents, preservatives, and other solubilizing agents. However, the presence of these contaminants virtually ensures the failure of any subsequent analysis of the sample by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Sample cleanup procedures, therefore, must be performed prior to MALDI-MS analysis. This paper reports a probe-surface derivatization method that greatly simplifies this sample preparation process. MALDI probes possessing self-assembled monolayers (SAMs) terminated with ionic functional groups can rapidly extract peptides/proteins via ionic interactions from < or = 1-microL volumes of sample solutions placed directly on their surface. We have found that MALDI probes modified in this manner are a practical solution for analyzing very small volumes of peptide/protein solutions contaminated with high levels of inorganic salts, buffers, detergents, chaotropic agents, and other solubilizing agents.

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