Purification of tetracysteine-tagged proteins by affinity. Chromatography using a non-fluorescent, photochemically stable bisarsenical affinity ligand

Lai Qiang Ying, Bruce Branchaud

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The use of genetically encoded small peptide tags such as polyhistidine and tetracysteine tags has become important for protein purification and enrichment. An improved affinity purification of tetracysteine (CCXXCC) tagged proteins has been achieved using a nonfluorescent, photochemically stable bisarsenical affinity ligand SplAsH. The photochemical stability of the SplAsHbiotin, shown in compound 5, is superior to FlAsH-EDT 2 and ReAsH-EDT 2. An application of the SplAsH tag for affinity purification of tetracysteine-tagged proteins is reported.

Original languageEnglish (US)
Pages (from-to)987-992
Number of pages6
JournalBioconjugate Chemistry
Volume22
Issue number5
DOIs
StatePublished - May 18 2011
Externally publishedYes

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Chromatography
Purification
Ligands
Proteins
Peptides

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Organic Chemistry
  • Pharmaceutical Science
  • Biomedical Engineering
  • Pharmacology

Cite this

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AB - The use of genetically encoded small peptide tags such as polyhistidine and tetracysteine tags has become important for protein purification and enrichment. An improved affinity purification of tetracysteine (CCXXCC) tagged proteins has been achieved using a nonfluorescent, photochemically stable bisarsenical affinity ligand SplAsH. The photochemical stability of the SplAsHbiotin, shown in compound 5, is superior to FlAsH-EDT 2 and ReAsH-EDT 2. An application of the SplAsH tag for affinity purification of tetracysteine-tagged proteins is reported.

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