期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1764, 期 10, 页码 1568-1576出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2006.07.009
关键词
disulfide bond; cyclic peptide; NMR spectroscopy; mass spectrometry
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. (c) 2006 Elsevier B.V. All rights reserved.
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