Publication Type:

Journal Article

Source:

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Volume 1764, Number 10, p.1568 - 1576 (2006)

URL:

http://www.sciencedirect.com/science/article/pii/S1570963906002494

Keywords:

mass spectrometry

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.

Cite this Research Publication

S. Sudarslal, Romanuka, J., Billeter, M., Skjeldal, L., Emmett, M. R., Nilsson, C. L., and Marshall, A. G., “Structural Characterization of an Unusually Stable Cyclic Peptide, Kalata \B2\ from Oldenlandia Affinis”, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol. 1764, pp. 1568 - 1576, 2006.

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