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Structural Characterization of an Unusually Stable Cyclic Peptide, Kalata B2 from Oldenlandia Affinis

Publication Type : Journal Article

Publisher : Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Campus : Amritapuri

School : School of Biotechnology

Center : Biotechnology

Year : 2006

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.

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