Diverse cyclic seed peptides in the Mexican zinnia (Zinnia haageana)

Franke, Bastian, Jayasena, Achala S., Fisher, Mark F., Swedberg, Joakim E., Taylor, Nicolas L., Mylne, Joshua S. and Rosengren, K. Johan (2016) Diverse cyclic seed peptides in the Mexican zinnia (Zinnia haageana). Biopolymers, 106 6: 806-817. doi:10.1002/bip.22901


Author Franke, Bastian
Jayasena, Achala S.
Fisher, Mark F.
Swedberg, Joakim E.
Taylor, Nicolas L.
Mylne, Joshua S.
Rosengren, K. Johan
Title Diverse cyclic seed peptides in the Mexican zinnia (Zinnia haageana)
Formatted title
Diverse cyclic seed peptides in the Mexican zinnia (Zinnia haageana)
Journal name Biopolymers   Check publisher's open access policy
ISSN 1097-0282
0006-3525
Publication date 2016-11-01
Year available 2016
Sub-type Article (original research)
DOI 10.1002/bip.22901
Open Access Status Not yet assessed
Volume 106
Issue 6
Start page 806
End page 817
Total pages 12
Place of publication Hoboken, NJ, United States
Publisher John Wiley & Sons
Language eng
Abstract A new family of small plant peptides was recently described and found to be widespread throughout the Millereae and Heliantheae tribes of the sunflower family Asteraceae. These peptides originate from the post-translational processing of unusual seed-storage albumin genes, and have been termed PawS-derived peptides (PDPs). The prototypic family member is a 14-residue cyclic peptide with potent trypsin inhibitory activity named SunFlower Trypsin Inhibitor (SFTI-1). In this study we present the features of three new PDPs discovered in the seeds of the sunflower species Zinnia haageana by a combination of de novo transcriptomics and liquid chromatography-mass spectrometry. Two-dimensional solution NMR spectroscopy was used to elucidate their structural characteristics. All three Z. haageana peptides have well-defined folds with a head-to-tail cyclized peptide backbone and a single disulfide bond. Although two possess an anti-parallel β-sheet structure, like SFTI-1, the Z. haageana peptide PDP-21 has a more irregular backbone structure. Despite structural similarities with SFTI-1, PDP-20 was not able to inhibit trypsin, thus the functional roles of these peptides is yet to be discovered. Defining the structural features of the small cyclic peptides found in the sunflower family will be useful for guiding the exploitation of these peptides as scaffolds for grafting and protein engineering applications.
Formatted abstract
A new family of small plant peptides was recently described and found to be widespread throughout the Millereae and Heliantheae tribes of the sunflower family Asteraceae. These peptides originate from the post-translational processing of unusual seed-storage albumin genes, and have been termed PawS-derived peptides (PDPs). The prototypic family member is a 14-residue cyclic peptide with potent trypsin inhibitory activity named SunFlower Trypsin Inhibitor (SFTI-1). In this study we present the features of three new PDPs discovered in the seeds of the sunflower species Zinnia haageana by a combination of de novo transcriptomics and liquid chromatography-mass spectrometry. Two-dimensional solution NMR spectroscopy was used to elucidate their structural characteristics. All three Z. haageana peptides have well-defined folds with a head-to-tail cyclized peptide backbone and a single disulfide bond. Although two possess an anti-parallel β-sheet structure, like SFTI-1, the Z. haageana peptide PDP-21 has a more irregular backbone structure. Despite structural similarities with SFTI-1, PDP-20 was not able to inhibit trypsin, thus the functional roles of these peptides is yet to be discovered. Defining the structural features of the small cyclic peptides found in the sunflower family will be useful for guiding the exploitation of these peptides as scaffolds for grafting and protein engineering applications.
Keyword Cyclic peptide
NMR spectroscopy
PawS-derived peptide (PDP)
Peptide structure
Sunflower trypsin inhibitor-1 (SFTI-1)
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID DP120103369
FT130100890
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 1 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 06 Dec 2016, 11:06:37 EST by System User on behalf of Learning and Research Services (UQ Library)