Platforms for enrichment of phosphorylated proteins and peptides in proteomics

Íris L Batalha, Christopher R Lowe, Ana Cecília Afonso Roque

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

Protein phosphorylation is a complex and highly dynamic process involved in numerous biological events. Abnormal phosphorylation is one of the underlying mechanisms for the development of cancer and metabolic disorders. The identification and absolute quantification of specific phospho-signatures can help elucidate protein functions in signaling pathways and facilitate the development of new and personalized diagnostic and therapeutic tools. This review presents a variety of strategies currently utilized for the enrichment of phosphorylated proteins and peptides before mass spectrometry analysis during proteomic studies. The investigation of specific affinity reagents, allied to the integration of different enrichment processes, is triggering the development of more selective, rapid and cost-effective high-throughput automated platforms.
Original languageEnglish
Pages (from-to)100-110
JournalTrends In Biotechnology
Volume30
Issue number2
DOIs
Publication statusPublished - 2012

Keywords

  • MASS-SPECTROMETRY ANALYSIS
  • MALDI-TOF-MS
  • PHOSPHOPROTEIN-BINDING-DOMAINS
  • COATED MAGNETIC NANOPARTICLES
  • CORE-SHELL MICROSPHERES
  • HIGHLY SPECIFIC CAPTURE
  • CODED AFFINITY TAGS
  • PHOSPHOPEPTIDE ENRICHMENT
  • ZIRCONIUM PHOSPHONATE
  • MOLECULAR RECOGNITION

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