Structural characterization of an unusually stable cyclic peptide, kalata B2 from Oldenlandia affinis

Sudarslal Sadasivan Nair, Julija Romanuka, Martin Billeter, Lars Skjeldal, Mark R. Emmett, Carol L. Nilsson, Alan G. Marshall

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

Kalata peptides are isolated from an African medicinal plant, Oldenlandia affinis, an aqueous decoction of which can be ingested to accelerate uterine contraction during childbirth. The closely packed disulfide core of kalata peptides confers unusual stability against thermal, chemical, and enzymatic degradation. The molecular arrangement may hamper NMR-assisted disulfide connectivity assignment. We have combined NMR with high-resolution mass spectrometry (MS) and MS/MS of native and chemically derivatized kalata B2 to determine its amino acid sequence and disulfide connectivity. Infrared multiphoton dissociation establishes the disulfide bond linkages in kalata B2 as I-IV, II-V and III-VI.

Original languageEnglish (US)
Pages (from-to)1568-1576
Number of pages9
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1764
Issue number10
DOIs
StatePublished - Oct 1 2006

Keywords

  • Cyclic peptide
  • Disulfide bond
  • Mass spectrometry
  • NMR spectroscopy

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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