Chemical synthesis of dendrotoxin-i: revision of the reported structure

H. Nishio, T. Inui, Y. Nishiuchi, C.L.C. De Medeiros, E.G. Rowan, A.L. Harvey, E. Katoh, T. Yamazaki

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Dendrotoxin I (DTX-I) is a 60-residue peptide from the venom of the black mamba snake Dendroaspis polylepis, which binds to neuronal K+ channels. The structure reported previously for DTX-I was synthesized for the first time by a solution procedure. The synthetic product was confirmed to have the correct primary and disulfide structure determined by peptide mapping, sequence analysis and mass measurements. Comparison of synthetic DTX-I with the natural one by high-performance liquid chromatography and capillary zone electrophoresis, as well as by sequence analysis, revealed that the Asn residue at position 12 in the synthetic peptide was Asp in the natural product. Synthesis of DTX-I with Asp at position 12 gave a peptide identical with the natural product in all aspects. NMR analysis of synthetic [Asn12]- and [Asp12]-DTX-I also supported our findings that the Asn residue at position 12 in the DTX-I molecule should be revised as Asp. [Asn12]- and [Asp12]-DTX-I had very similar binding affinities when tested against radiolabeled dendrotoxin binding to rat brain synaptosomal membranes.
Original languageEnglish
Pages (from-to)355-364
Number of pages9
JournalJournal of Peptide Research
Volume51
Issue number5
DOIs
Publication statusPublished - May 1998

Keywords

  • chemical synthesis
  • dendrotoxin I
  • NMR analysis
  • potassium channel blocker
  • receptor binding assay
  • revised structure

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