RT Journal Article
SR Electronic
T1 Structural Characterization of the PawL-Derived Peptide Family, an Ancient Subfamily of Orbitides
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.07.18.452857
DO 10.1101/2021.07.18.452857
A1 Colton D. Payne
A1 Mark F. Fisher
A1 Joshua S. Mylne
A1 K. Johan Rosengren
YR 2021
UL http://biorxiv.org/content/early/2021/09/21/2021.07.18.452857.abstract
AB Plants are an excellent source of bioactive peptides, often with disulfide bonds and/or a cyclic backbone. While focus has predominantly been directed at disulfide-rich peptides, a large family of small, cyclic but non-disulfide bonded plant peptides, known as orbitides, has been relatively ignored. A recently discovered subfamily of orbitides is the PawL-Derived Peptides (PLPs), produced during the maturation of precursors for seed storage albumins. Although their evolutionary origins have been dated, in-depth exploration of the family’s structural characteristics and potential bioactivities remains to be conducted. Here we present an extensive and systematic characterization of the PLP family. Nine PLPs were chosen and prepared by solid phase peptide synthesis. Their structural features were studied using solution NMR spectroscopy and seven were found to possess regions of backbone order. Ordered regions consist of β-turns, with some PLPs adopting two well-defined β-turns within sequences as short as seven residues, which are largely the result of side chain interactions. Our data highlight that the sequence diversity within this family results in equally diverse molecular scaffolds. None of these nine PLPs showed antibacterial or antifungal activity.Competing Interest StatementThe authors have declared no competing interest.