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Related Experiment Video

Updated: Mar 14, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

Natural structural diversity within a conserved cyclic peptide scaffold.

Alysha G Elliott¹, Bastian Franke², David A Armstrong²

¹Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.

|October 4, 2016

Summary

Researchers discovered a new family of plant peptides, the PawS derived peptides (PDPs), with diverse structures and potential as drug scaffolds. These small, disulfide-bonded peptides, including sunflower trypsin inhibitor-1, show sequence-dependent variations in conformation and properties.

Keywords:

Cyclic peptide PawS derived peptide (PDP)Peptide structure Solution NMR spectroscopy Sunflower trypsin inhibitor-1 (SFTI-1)

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Last Updated: Mar 14, 2026

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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

Area of Science:

Biochemistry
Structural Biology
Plant Science

Background:

A diverse class of small, single-disulfide bonded peptides derived from Preproalbumin with SFTI-1 (PawS1) proteins has been identified in flowering plant seeds (Asteraceae).
The founding member, sunflower trypsin inhibitor-1 (SFTI-1), is a potent trypsin inhibitor from Helianthus annuus.

Purpose of the Study:

To detail the structural diversity of the PawS derived peptide (PDP) family.
To investigate the conformational characteristics influenced by sequence variations in these peptides.

Main Methods:

Solution Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine peptide structures.
Analysis of side-chain projections, flexibility, and physicochemical properties was conducted.

Main Results:

Multiple structures of PDPs were elucidated, revealing a conserved backbone framework with a single disulfide bond.
Many PDPs exhibit head-to-tail backbone cyclization.
Significant structural diversity exists due to variations in amino acid sequences, affecting side-chain projections and flexibility.

Conclusions:

The PDP family represents a structurally diverse group of small peptides with unique characteristics.
Amino acid side-chains play a crucial role in fine-tuning the conformations of these cyclic peptides.
These findings highlight the potential of PDPs as promising scaffolds for drug development in the pharmaceutical industry.