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Title of Journal: Amino Acids

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Abbravation: Amino Acids

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Springer Vienna

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ISSN

1438-2199

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Natural structural diversity within a conserved cy

Authors: Alysha G Elliott Bastian Franke David A Armstrong David J Craik Joshua S Mylne K Johan Rosengren
Publish Date: 2016/10/01
Volume: 49, Issue: 1, Pages: 103-116
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Abstract

We recently isolated and described the evolutionary origin of a diverse class of small singledisulfide bonded peptides derived from Preproalbumin with SFTI1 PawS1 proteins in the seeds of flowering plants Asteraceae The founding member of the PawS derived peptide PDP family is the potent trypsin inhibitor SFTI1 sunflower trypsin inhibitor1 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 headtotail cyclized backbone they all have their own characteristics in terms of projections of sidechains 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 sidechains can finetune conformations in these promising peptides

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