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Figure 1

Nature Biotechnology  23, 463 - 468 (2005)
Published online: 13 March 2005; | doi:10.1038/nbt1076

Enrichment and analysis of peptide subsets using fluorous affinity tags and mass spectrometry

Scott M Brittain, Scott B Ficarro, Ansgar Brock & Eric C Peters
 
Fig 1 full size
Figure 1. Fluorous proteomics strategy for the isolation of specific classes of peptides.
(a) Depiction of the overall method. A specific peptide class is selectively labeled with a fluorous tag ('F') bearing the appropriate functional group (for example, a thiol group to effect Michael addition after beta-elimination) and isolated using fluorous solid-phase extraction, followed by MALDI-MS or ESI-MS analysis. (b) MALDI-MS spectrum of alpha-casein tryptic digest spiked with fluorous domain−containing peptides. (c) Nontagged peptides are observed in the MALDI-MS spectrum of the FSPE flow-through fraction. (d) Fluorous-tagged peptides are observed in the MALDI-MS spectrum of the FSPE elution fraction. q, pyroglutamic acid; s F17, dehydroalanine residue after reaction with 1H,1H,2H,2H-perfluorodecane-1-thiol.

 
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