Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/142743
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dc.contributor.authorZhang, Si Minen_US
dc.contributor.authorLiao, Yingen_US
dc.contributor.authorNeo, Tuan Lingen_US
dc.contributor.authorLu, Yanningen_US
dc.contributor.authorLiu, Ding Xiangen_US
dc.contributor.authorVahlne, Andersen_US
dc.contributor.authorTam, James Pingkwanen_US
dc.date.accessioned2020-06-29T09:37:24Z-
dc.date.available2020-06-29T09:37:24Z-
dc.date.issued2018-
dc.identifier.citationZhang, S. M., Liao, Y., Neo, T. L., Lu, Y., Liu, D. X., Vahlne, A., & Tam, J. P. (2018). Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein. International Journal of Biochemistry and Cell Biology, 101, 103-112. doi:10.1016/j.biocel.2018.05.012en_US
dc.identifier.issn1357-2725en_US
dc.identifier.urihttps://hdl.handle.net/10356/142743-
dc.description.abstractSelf-binding peptides containing zipper-like sequences, such as the Leu/Ile zipper sequence within the coiled coil regions of proteins and the cross-β spine steric zippers within the amyloid-like fibrils, could bind to the protein-of-origin through homophilic sequence-specific zipper motifs. These self-binding sequences represent opportunities for the development of biochemical tools and/or therapeutics. Here, we report on the identification of a putative self-binding β-zipper-forming peptide within the severe acute respiratory syndrome-associated coronavirus spike (S) protein and its application in viral detection. Peptide array scanning of overlapping peptides covering the entire length of S protein identified 34 putative self-binding peptides of six clusters, five of which contained octapeptide core consensus sequences. The Cluster I consensus octapeptide sequence GINITNFR was predicted by the Eisenberg's 3D profile method to have high amyloid-like fibrillation potential through steric β-zipper formation. Peptide C6 containing the Cluster I consensus sequence was shown to oligomerize and form amyloid-like fibrils. Taking advantage of this, C6 was further applied to detect the S protein expression in vitro by fluorescence staining. Meanwhile, the coiled-coil-forming Leu/Ile heptad repeat sequences within the S protein were under-represented during peptide array scanning, in agreement with that long peptide lengths were required to attain high helix-mediated interaction avidity. The data suggest that short β-zipper-like self-binding peptides within the S protein could be identified through combining the peptide scanning and predictive methods, and could be exploited as biochemical detection reagents for viral infection.en_US
dc.description.sponsorshipMOE (Min. of Education, S’pore)en_US
dc.language.isoenen_US
dc.relation.ispartofInternational Journal of Biochemistry and Cell Biologyen_US
dc.rights© 2018 Elsevier Ltd. All rights reserved.en_US
dc.subjectScience::Biological sciencesen_US
dc.titleIdentification and application of self-binding zipper-like sequences in SARS-CoV spike proteinen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doi10.1016/j.biocel.2018.05.012-
dc.identifier.pmid29800727-
dc.identifier.scopus2-s2.0-85048111699-
dc.identifier.volume101en_US
dc.identifier.spage103en_US
dc.identifier.epage112en_US
dc.subject.keywordsSteric β-zipperen_US
dc.subject.keywordsSARS-CoV Spike Proteinen_US
item.grantfulltextnone-
item.fulltextNo Fulltext-
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