Natural structural diversity within a conserved cyclic peptide scaffold

Elliott, Alysha G., Franke, Bastian, Armstrong, David A., Craik, David J., Mylne, Joshua S. and Rosengren, K. Johan (2016) Natural structural diversity within a conserved cyclic peptide scaffold. Amino Acids, 49 1: 1-14. doi:10.1007/s00726-016-2333-x


Author Elliott, Alysha G.
Franke, Bastian
Armstrong, David A.
Craik, David J.
Mylne, Joshua S.
Rosengren, K. Johan
Title Natural structural diversity within a conserved cyclic peptide scaffold
Journal name Amino Acids   Check publisher's open access policy
ISSN 1438-2199
0939-4451
Publication date 2016-01-01
Year available 2016
Sub-type Article (original research)
DOI 10.1007/s00726-016-2333-x
Open Access Status Not yet assessed
Volume 49
Issue 1
Start page 1
End page 14
Total pages 14
Place of publication Wien, Austria
Publisher Springer Wien
Language eng
Subject 1303 Biochemistry
1308 Clinical Biochemistry
1605 Organic Chemistry
Abstract We recently isolated and described the evolutionary origin of a diverse class of small single-disulfide bonded peptides derived from Preproalbumin with SFTI-1 (PawS1) proteins in the seeds of flowering plants (Asteraceae). The founding member of the PawS derived peptide (PDP) family is the potent trypsin inhibitor SFTI-1 (sunflower trypsin inhibitor-1) from Helianthus annuus, the common sunflower. Here we provide additional structures and describe the structural diversity of this new class of small peptides, derived from solution NMR studies, in detail. We show that although most have a similar backbone framework with a single disulfide bond and in many cases a head-to-tail cyclized backbone, they all have their own characteristics in terms of projections of side-chains, flexibility and physiochemical properties, attributed to the variety of their sequences. Small cyclic and constrained peptides are popular as drug scaffolds in the pharmaceutical industry and our data highlight how amino acid side-chains can fine-tune conformations in these promising peptides.
Formatted abstract
We recently isolated and described the evolutionary origin of a diverse class of small single-disulfide bonded peptides derived from Preproalbumin with SFTI-1 (PawS1) proteins in the seeds of flowering plants (Asteraceae). The founding member of the PawS derived peptide (PDP) family is the potent trypsin inhibitor SFTI-1 (sunflower trypsin inhibitor-1) from Helianthus annuus, the common sunflower. Here we provide additional structures and describe the structural diversity of this new class of small peptides, derived from solution NMR studies, in detail. We show that although most have a similar backbone framework with a single disulfide bond and in many cases a head-to-tail cyclized backbone, they all have their own characteristics in terms of projections of side-chains, flexibility and physiochemical properties, attributed to the variety of their sequences. Small cyclic and constrained peptides are popular as drug scaffolds in the pharmaceutical industry and our data highlight how amino acid side-chains can fine-tune conformations in these promising peptides.
Keyword Sunflower trypsin inhibitor-1 (SFTI-1)
PawS derived peptide (PDP)
Cyclic peptide
Solution NMR spectroscopy
Peptide structure
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID DP120103369
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
 
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