Natural structural diversity within a conserved cyclic peptide scaffold

Alysha G. Elliott, Bastian Franke, David A. Armstrong, David J. Craik, Joshua S. Mylne, K. Johan Rosengren

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)103-116
Number of pages14
JournalAmino Acids
Volume49
Issue number1
DOIs
Publication statusPublished - 1 Jan 2017

Fingerprint

Cyclic Peptides
Scaffolds
Peptides
Helianthus
Disulfides
Asteraceae
Trypsin Inhibitors
Drug Industry
Pharmaceutical Preparations
Seed
Conformations
Seeds
Nuclear magnetic resonance
Amino Acids
Industry
Proteins
sunflower SFTI-1 peptide

Cite this

Elliott, A. G., Franke, B., Armstrong, D. A., Craik, D. J., Mylne, J. S., & Rosengren, K. J. (2017). Natural structural diversity within a conserved cyclic peptide scaffold. Amino Acids, 49(1), 103-116. https://doi.org/10.1007/s00726-016-2333-x
Elliott, Alysha G. ; Franke, Bastian ; Armstrong, David A. ; Craik, David J. ; Mylne, Joshua S. ; Rosengren, K. Johan. / Natural structural diversity within a conserved cyclic peptide scaffold. In: Amino Acids. 2017 ; Vol. 49, No. 1. pp. 103-116.
@article{bd73999e59d14032b697b2fbf99e18ff,
title = "Natural structural diversity within a conserved cyclic peptide scaffold",
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.",
keywords = "Cyclic peptide, PawS derived peptide (PDP), Peptide structure, Solution NMR spectroscopy, Sunflower trypsin inhibitor-1 (SFTI-1)",
author = "Elliott, {Alysha G.} and Bastian Franke and Armstrong, {David A.} and Craik, {David J.} and Mylne, {Joshua S.} and Rosengren, {K. Johan}",
year = "2017",
month = "1",
day = "1",
doi = "10.1007/s00726-016-2333-x",
language = "English",
volume = "49",
pages = "103--116",
journal = "Amino Acids",
issn = "0939-4451",
publisher = "Springer",
number = "1",

}

Elliott, AG, Franke, B, Armstrong, DA, Craik, DJ, Mylne, JS & Rosengren, KJ 2017, 'Natural structural diversity within a conserved cyclic peptide scaffold' Amino Acids, vol. 49, no. 1, pp. 103-116. https://doi.org/10.1007/s00726-016-2333-x

Natural structural diversity within a conserved cyclic peptide scaffold. / Elliott, Alysha G.; Franke, Bastian; Armstrong, David A.; Craik, David J.; Mylne, Joshua S.; Rosengren, K. Johan.

In: Amino Acids, Vol. 49, No. 1, 01.01.2017, p. 103-116.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Natural structural diversity within a conserved cyclic peptide scaffold

AU - Elliott, Alysha G.

AU - Franke, Bastian

AU - Armstrong, David A.

AU - Craik, David J.

AU - Mylne, Joshua S.

AU - Rosengren, K. Johan

PY - 2017/1/1

Y1 - 2017/1/1

N2 - 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.

AB - 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.

KW - Cyclic peptide

KW - PawS derived peptide (PDP)

KW - Peptide structure

KW - Solution NMR spectroscopy

KW - Sunflower trypsin inhibitor-1 (SFTI-1)

UR - http://www.scopus.com/inward/record.url?scp=84989180833&partnerID=8YFLogxK

U2 - 10.1007/s00726-016-2333-x

DO - 10.1007/s00726-016-2333-x

M3 - Article

VL - 49

SP - 103

EP - 116

JO - Amino Acids

JF - Amino Acids

SN - 0939-4451

IS - 1

ER -

Elliott AG, Franke B, Armstrong DA, Craik DJ, Mylne JS, Rosengren KJ. Natural structural diversity within a conserved cyclic peptide scaffold. Amino Acids. 2017 Jan 1;49(1):103-116. https://doi.org/10.1007/s00726-016-2333-x