Structural characterization of an unusually stable cyclic peptide, kalata B2 from Oldenlandia affinis
(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.
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https://lup.lub.lu.se/record/eb781420-3014-4552-a80d-e030481d0be3
- author
- Nair, Sudarslal Sadasivan ; Romanuka, Julija ; Billeter, Martin ; Skjeldal, Lars ; Emmett, Mark R ; Nilsson, Carol L LU and Marshall, Alan G
- publishing date
- 2006-10
- 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
-
- scopus:33749649874
- pmid:16987719
- 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
- 2024-10-14 06:11:06
@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}}, }