Production of recombinant Conkunitzin-S1 in Escherichia coli

Monika Bayrhuber, Roland Graf, Michael Ferber, Markus Zweckstetter, Julita Imperial, James E. Garrett, Baldomero M. Olivera, Heinrich Terlau, Stefan Becker*

*Corresponding author for this work
15 Citations (Scopus)


Conkunitzin-S1 from the cone snail Conus striatus is the first member of a new neurotoxin family with a canonical Kunitz domain fold. Conk-S1 is 60 amino acids long and lacks one of the three conserved disulfide bonds typically found in Kunitz domain modules. It binds specifically to voltage activated potassium channels of the Shaker family. The peptide was expressed in insoluble form in fusion with an N-terminal intein. Refolding in the presence of glutathione followed by pH shift-induced cleavage of the fusion protein resulted in a functional toxin as demonstrated by voltage-clamp measurements.

Original languageEnglish
JournalProtein Expression and Purification
Issue number2
Pages (from-to)640-644
Number of pages5
Publication statusPublished - 01.06.2006

Research Areas and Centers

  • Academic Focus: Center for Brain, Behavior and Metabolism (CBBM)


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