Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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

Nair, Sudarslal Sadasivan ; Romanuka, Julija ; Billeter, Martin ; Skjeldal, Lars ; Emmett, Mark R ; Nilsson, Carol L LU and Marshall, Alan G (2006) In Biochimica et Biophysica Acta 1764(10). p.76-1568
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.

Please use this url to cite or link to this publication:
author
; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Amino Acid Sequence, Cyclotides, Mass Spectrometry, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oldenlandia, Peptides, Cyclic, Protein Conformation, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
in
Biochimica et Biophysica Acta
volume
1764
issue
10
pages
9 pages
publisher
Elsevier
external identifiers
  • pmid:16987719
  • scopus:33749649874
ISSN
0006-3002
DOI
10.1016/j.bbapap.2006.07.009
language
English
LU publication?
no
id
eb781420-3014-4552-a80d-e030481d0be3
date added to LUP
2017-05-16 10:34:42
date last changed
2024-05-26 15:43:48
@article{eb781420-3014-4552-a80d-e030481d0be3,
  abstract     = {{<p>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.</p>}},
  author       = {{Nair, Sudarslal Sadasivan and Romanuka, Julija and Billeter, Martin and Skjeldal, Lars and Emmett, Mark R and Nilsson, Carol L and Marshall, Alan G}},
  issn         = {{0006-3002}},
  keywords     = {{Amino Acid Sequence; Cyclotides; Mass Spectrometry; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Oldenlandia; Peptides, Cyclic; Protein Conformation; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{76--1568}},
  publisher    = {{Elsevier}},
  series       = {{Biochimica et Biophysica Acta}},
  title        = {{Structural characterization of an unusually stable cyclic peptide, kalata B2 from Oldenlandia affinis}},
  url          = {{http://dx.doi.org/10.1016/j.bbapap.2006.07.009}},
  doi          = {{10.1016/j.bbapap.2006.07.009}},
  volume       = {{1764}},
  year         = {{2006}},
}