dc.contributor.authorTam, James P.
dc.contributor.authorNguyen, Giang Kien Truc
dc.contributor.authorLoo, Shining
dc.contributor.authorWang, Shujing
dc.contributor.authorYang, Daiwen
dc.contributor.authorKam, Antony
dc.date.accessioned2019-01-11T06:34:30Z
dc.date.available2019-01-11T06:34:30Z
dc.date.issued2018
dc.identifier.citationTam, J. P., Nguyen, G. K. T., Loo, S., Wang, S., Yang, D., & Kam, A. (2018). Ginsentides : cysteine and glycine-rich peptides from the ginseng family with unusual disulfide connectivity. Scientific Reports, 8(1), 16201-. doi:10.1038/s41598-018-33894-xen_US
dc.identifier.urihttp://hdl.handle.net/10220/47447
dc.description.abstractGinseng, a popular and valuable traditional medicine, has been used for centuries to maintain health and treat disease. Here we report the discovery and characterization of ginsentides, a novel family of cysteine and glycine-rich peptides derived from the three most widely-used ginseng species: Panax ginseng, Panax quinquefolius, and Panax notoginseng. Using proteomic and transcriptomic methods, we identified 14 ginsentides, TP1-TP14 which consist of 31–33 amino acids and whose expression profiles are species- and tissues-dependent. Ginsentides have an eight-cysteine motif typical of the eight-cysteine-hevein-like peptides (8C-HLP) commonly found in medicinal herbs, but lack a chitin-binding domain. Transcriptomic analysis showed that the three-domain biosynthetic precursors of ginsentides differ from known 8C-HLP precursors in architecture and the absence of a C-terminal protein-cargo domain. A database search revealed an additional 50 ginsentide-like precursors from both gymnosperms and angiosperms. Disulfide mapping and structure determination of the ginsentide TP1 revealed a novel disulfide connectivity that differs from the 8C-HLPs. The structure of ginsentide TP1 is highly compact, with the N- and C-termini topologically fixed by disulfide bonds to form a pseudocyclic structure that confers resistance to heat, proteolysis, and acid and serum-mediated degradation. Together, our results expand the chemical space of natural products found in ginseng and highlight the occurrence, distribution, disulfide connectivity, and precursor architectures of cysteine- and glycine-rich ginsentides as a class of novel non-chitin-binding, non-cargo-carrying 8C-HLPs.en_US
dc.description.sponsorshipMOE (Min. of Education, S’pore)en_US
dc.format.extent15 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesScientific Reportsen_US
dc.rights© 2018 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.en_US
dc.subjectGinsengen_US
dc.subjectDisulfide Connectivityen_US
dc.subjectDRNTU::Science::Biological sciencesen_US
dc.titleGinsentides : cysteine and glycine-rich peptides from the ginseng family with unusual disulfide connectivityen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1038/s41598-018-33894-x
dc.description.versionPublished versionen_US


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