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

doi:10.1016/j.bbapap.2006.07.009

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 journal › Article › peer-review

30 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 language	English (US)
Pages (from-to)	1568-1576
Number of pages	9
Journal	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1764
Issue number	10
DOIs	https://doi.org/10.1016/j.bbapap.2006.07.009
State	Published - Oct 2006
Externally published	Yes

Keywords

Cyclic peptide
Disulfide bond
Mass spectrometry
NMR spectroscopy

ASJC Scopus subject areas

Analytical Chemistry
Biophysics
Biochemistry
Molecular Biology

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10.1016/j.bbapap.2006.07.009

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

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.",

keywords = "Cyclic peptide, Disulfide bond, Mass spectrometry, NMR spectroscopy",

author = "Nair, {Sudarslal Sadasivan} and Julija Romanuka and Martin Billeter and Lars Skjeldal and Emmett, {Mark R.} and Nilsson, {Carol L.} and Marshall, {Alan G.}",

note = "Funding Information: We thank Christopher L. Hendrickson, Gregory T. Blakney, John P. Quinn, Yury O. Tsybin and Kim F. Haselmann, for valuable discussions and suggestions. We gratefully acknowledge the financial support of the NSF National High-Field FT-ICR Mass Spectrometry Facility (DMR 00-84173), the Swedish Foundation for International Cooperation in Research and Higher Education (STINT) and the Swedish National Research Council (Vetenskapsr{\aa}det-Medicin). JR and MB thank the Swedish Research Council (VR grant 621-2003-4048), the Swedish NMR Centre and Chalmers Technical University (International Masters' Program) for support. JR is grateful for support through a scholarship from The Swedish Institute. ",

year = "2006",

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doi = "10.1016/j.bbapap.2006.07.009",

language = "English (US)",

volume = "1764",

pages = "1568--1576",

journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",

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T1 - Structural characterization of an unusually stable cyclic peptide, kalata B2 from Oldenlandia affinis

AU - Nair, Sudarslal Sadasivan

AU - Romanuka, Julija

AU - Billeter, Martin

AU - Skjeldal, Lars

AU - Emmett, Mark R.

AU - Nilsson, Carol L.

AU - Marshall, Alan G.

N1 - Funding Information: We thank Christopher L. Hendrickson, Gregory T. Blakney, John P. Quinn, Yury O. Tsybin and Kim F. Haselmann, for valuable discussions and suggestions. We gratefully acknowledge the financial support of the NSF National High-Field FT-ICR Mass Spectrometry Facility (DMR 00-84173), the Swedish Foundation for International Cooperation in Research and Higher Education (STINT) and the Swedish National Research Council (Vetenskapsrådet-Medicin). JR and MB thank the Swedish Research Council (VR grant 621-2003-4048), the Swedish NMR Centre and Chalmers Technical University (International Masters' Program) for support. JR is grateful for support through a scholarship from The Swedish Institute.

PY - 2006/10

Y1 - 2006/10

N2 - 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.

AB - 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.

KW - Cyclic peptide

KW - Disulfide bond

KW - Mass spectrometry

KW - NMR spectroscopy

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

Abstract

Keywords

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