Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/85406
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dc.contributor.authorNguyen, Giang Kien Trucen
dc.contributor.authorTam, James Pingkwanen
dc.contributor.authorLoo, Shiningen
dc.contributor.authorKam, Antonyen
dc.contributor.authorXiao, Tianshuen
dc.contributor.authorLiu, Chuan Faen
dc.date.accessioned2018-11-22T02:55:26Zen
dc.date.accessioned2019-12-06T16:03:11Z-
dc.date.available2018-11-22T02:55:26Zen
dc.date.available2019-12-06T16:03:11Z-
dc.date.issued2016en
dc.identifier.citationLoo, S., Kam, A., Xiao, T., Nguyen, G. K. T., Liu, C. F., & Tam, J. P. (2016). Identification and characterization of roseltide, a knottin-type neutrophil elastase inhibitor derived from hibiscus sabdariffa. Scientific Reports, 6, 39401-. doi:10.1038/srep39401en
dc.identifier.urihttps://hdl.handle.net/10356/85406-
dc.description.abstractPlant knottins are of therapeutic interest due to their high metabolic stability and inhibitory activity against proteinases involved in human diseases. The only knottin-type proteinase inhibitor against porcine pancreatic elastase was first identified from the squash family in 1989. Here, we report the identification and characterization of a knottin-type human neutrophil elastase inhibitor from Hibiscus sabdariffa of the Malvaceae family. Combining proteomic and transcriptomic methods, we identified a panel of novel cysteine-rich peptides, roseltides (rT1-rT8), which range from 27 to 39 residues with six conserved cysteine residues. The 27-residue roseltide rT1 contains a cysteine spacing and amino acid sequence that is different from the squash knottin-type elastase inhibitor. NMR analysis demonstrated that roseltide rT1 adopts a cystine-knot fold. Transcriptome analyses suggested that roseltides are bioprocessed by asparagine endopeptidases from a three-domain precursor. The cystine-knot structure of roseltide rT1 confers its high resistance against degradation by endopeptidases, 0.2 N HCl, and human serum. Roseltide rT1 was shown to inhibit human neutrophil elastase using enzymatic and pull-down assays. Additionally, roseltide rT1 ameliorates neutrophil elastase-stimulated cAMP accumulation in vitro. Taken together, our findings demonstrate that roseltide rT1 is a novel knottin-type neutrophil elastase inhibitor with therapeutic potential for neutrophil elastase associated diseases.en
dc.description.sponsorshipNRF (Natl Research Foundation, S’pore)en
dc.format.extent16 p.en
dc.language.isoenen
dc.relation.ispartofseriesScientific Reportsen
dc.rights© 2016 The Authors (Nature Publishing Group). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/en
dc.subjectNeutrophilen
dc.subjectLeukocyte Elastase Inhibitoren
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleIdentification and characterization of roseltide, a knottin-type neutrophil elastase inhibitor derived from hibiscus sabdariffaen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1038/srep39401en
dc.description.versionPublished versionen
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item.grantfulltextopen-
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