Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-018-33894-x
Title: Ginsentides: Cysteine and Glycine-rich Peptides from the Ginseng Family with Unusual Disulfide Connectivity
Authors: Tam, J.P
Nguyen, G.K.T
Loo, S
Wang, S
Yang, D 
Kam, A
Keywords: antimicrobial cationic peptide
cysteine
disulfide
glycine
hevein
peptide
plant lectin
proteome
transcriptome
chemical structure
chemistry
gene expression regulation
genetics
Panax
Panax notoginseng
Antimicrobial Cationic Peptides
Cysteine
Disulfides
Gene Expression Regulation, Plant
Glycine
Molecular Structure
Panax
Panax notoginseng
Peptides
Plant Lectins
Proteome
Transcriptome
Issue Date: 2018
Publisher: Nature Publishing Group
Citation: Tam, 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. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-018-33894-x
Rights: Attribution 4.0 International
Abstract: Ginseng, 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. © 2018, The Author(s).
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/178385
ISSN: 2045-2322
DOI: 10.1038/s41598-018-33894-x
Rights: Attribution 4.0 International
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
10_1038_s41598-018-33894-x.pdf6.22 MBAdobe PDF

OPEN

NoneView/Download

SCOPUSTM   
Citations

7
checked on Nov 27, 2020

Page view(s)

14
checked on Nov 26, 2020

Google ScholarTM

Check

Altmetric


This item is licensed under a Creative Commons License Creative Commons