dc.contributor.authorWong, Ka Ho
dc.contributor.authorTan, Wei Liang
dc.contributor.authorKini, Shruthi Gopalkrishna
dc.contributor.authorXiao, Tianshu
dc.contributor.authorSerra, Aida
dc.contributor.authorSze, Siu Kwan
dc.contributor.authorTam, James Pingkwan
dc.date.accessioned2017-12-21T02:35:03Z
dc.date.available2017-12-21T02:35:03Z
dc.date.issued2017
dc.identifier.citationWong, K. H., Tan, W. L., Kini, S. G., Xiao, T., Serra, A., Sze, S. K., et al. (2017). Vaccatides: Antifungal Glutamine-Rich Hevein-Like Peptides from Vaccaria hispanica. Frontiers in Plant Science, 8, 1100-.en_US
dc.identifier.urihttp://hdl.handle.net/10220/44179
dc.description.abstractHevein and hevein-like peptides are disulfide-constrained chitin-binding cysteine-rich peptides. They are divided into three subfamilies, 6C-, 8C-, and 10C-hevein-like peptides, based on the number of cysteine residues. In addition, hevein-like peptides can exist in two forms, short and long. The long C-terminal form found in hevein and 10C-hevein-like peptides contain a C-terminal protein cargo. In contrast, the short form without a protein cargo is found in all three subfamilies. Here, we report the discovery and characterization of two novel glutamine-rich and protein cargo-free 8C-hevein-like peptides, vaccatides vH1 and vH2, from Vaccaria hispanica of the Caryophyllaceae family. Proteomic analyses showed that the vaccatides are 40–41 amino acids in length and contain a chitin-binding domain. NMR determination revealed that vaccatide vH2 displays a highly compact structure with a N-terminal cystine knot and an addition C-terminal disulfide bond. Stability studies showed that this compact structure renders vaccatide vH2 resistant to thermal, chemical and proteolytic degradation. The chitin-binding vH2 was shown to inhibit the mycelium growth of four phyto-pathogenic fungal strains with IC50 values in the micromolar range. Our findings show that vaccatides represent a new family of 8C-hevein-like peptides, which are protein cargo-free and glutamine-rich, characteristics that differentiate them from the prototypic hevein and the 10C-hevein-like peptides. In summary, this study enriches the existing library of hevein-like peptides and provides insight into their molecular diversity in sequence, structure and biosynthesis. Additionally, their highly disulfide-constrained structure could be used as a scaffold for developing metabolically and orally active peptidyl therapeutics.en_US
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en_US
dc.format.extent14 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesFrontiers in Plant Scienceen_US
dc.rights© 2017 Wong, Tan, Kini, Xiao, Serra, Sze and Tam. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en_US
dc.subjectVaccaria Hispanicaen_US
dc.subjectHevein-like Peptidesen_US
dc.titleVaccatides: Antifungal Glutamine-Rich Hevein-Like Peptides from Vaccaria hispanicaen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.3389/fpls.2017.01100
dc.description.versionPublished versionen_US


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