Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
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.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.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.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.subject.keywordsSteric β-zipperen_US
dc.subject.keywordsSARS-CoV Spike Proteinen_US
item.fulltextNo Fulltext-
Appears in Collections:SBS Journal Articles

Citations 50

Updated on Jan 31, 2023

Web of ScienceTM
Citations 50

Updated on Jan 31, 2023

Page view(s)

Updated on Feb 4, 2023

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.