Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81859
Title: Cysteine-Rich Peptide Family with Unusual Disulfide Connectivity from Jasminum sambac
Authors: Kumari, Geeta
Serra, Aida
Shin, Joon
Nguyen, Phuong Q. T.
Sze, Siu Kwan
Yoon, Ho Sup
Tam, James P.
Keywords: signal peptide
Escherichia coli
Issue Date: 2015
Source: Kumari, G., Serra, A., Shin, J., Nguyen, P. Q. T., Sze, S. K., Yoon, H. S., & Tam, J. P. (2015). Cysteine-Rich Peptide Family with Unusual Disulfide Connectivity from Jasminum sambac. Journal of Natural Products, 78(11), 2791-2799.
Series/Report no.: Journal of Natural Products
Abstract: Cysteine-rich peptides (CRPs) are natural products with privileged peptidyl structures that represent a potentially rich source of bioactive compounds. Here, the discovery and characterization of a novel plant CRP family, jasmintides from Jasminum sambac of the Oleaceae family, are described. Two 27-amino acid jasmintides (jS1 and jS2) were identified at the gene and protein levels. Disulfide bond mapping of jS1 by mass spectrometry and its confirmation by NMR spectroscopy revealed disulfide bond connectivity of C-1-C-5, C-2-C-4, and C-3-C-6, a cystine motif that has not been reported in plant CRPs. Structural determination showed that jS1 displays a well-defined structure framed by three short antiparallel β-sheets. Genomic analysis showed that jasmintides share a three-domain precursor arrangement with a C-terminal mature domain preceded by a long pro-domain of 46 residues and an intron cleavage site between the signal sequence and pro-domain. The compact cysteine-rich structure together with an N-terminal pyroglutamic acid residue confers jasmintides high resistance to heat and enzymatic degradation, including exopeptidase treatment. Collectively, these results reveal a new plant CRP structure with an unusual cystine connectivity, which could be useful as a scaffold for designing peptide drugs.
URI: https://hdl.handle.net/10356/81859
http://hdl.handle.net/10220/39734
ISSN: 0163-3864
DOI: 10.1021/acs.jnatprod.5b00762
Rights: © 2015 The American Chemical Society and American Society of Pharmacognosy. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Natural Products, 2015 The American Chemical Society and American Society of Pharmacognosy. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1021/acs.jnatprod.5b00762].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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