dc.contributor.authorKumari, Geeta
dc.contributor.authorSerra, Aida
dc.contributor.authorShin, Joon
dc.contributor.authorNguyen, Phuong Q. T.
dc.contributor.authorSze, Siu Kwan
dc.contributor.authorYoon, Ho Sup
dc.contributor.authorTam, James P.
dc.date.accessioned2016-01-21T03:39:51Z
dc.date.available2016-01-21T03:39:51Z
dc.date.issued2015
dc.identifier.citationKumari, 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.en_US
dc.identifier.issn0163-3864en_US
dc.identifier.urihttp://hdl.handle.net/10220/39734
dc.description.abstractCysteine-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.en_US
dc.format.extent33 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesJournal of Natural Productsen_US
dc.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].en_US
dc.subjectsignal peptide
dc.subjectEscherichia coli
dc.titleCysteine-Rich Peptide Family with Unusual Disulfide Connectivity from Jasminum sambacen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1021/acs.jnatprod.5b00762
dc.description.versionAccepted versionen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record