Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 13, Pages 3941-3945Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201411232
Keywords
affinity reagents; proteins; proteomics; pyrophosphorylation; signal transduction
Categories
Funding
- NIH [DP2 CA186753]
- Princeton University
- NATIONAL CANCER INSTITUTE [DP2CA186753] Funding Source: NIH RePORTER
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A resin-bound dinuclear zinc(II) complex for the selective capture of pyrophosphopeptides is reported. The metal complex binds diphosphate esters over other anionic groups, such as monophosphate esters, sulfate esters, and carboxylic acids, with high specificity. Immobilization of the compound provided a reagent capable of binding and retaining nanomolar quantities of pyrophosphopeptide in the presence of cell lysate. The high affinity and specificity of the reagent makes it an attractive tool for the study of in vivo pyrophosphorylation.
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