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dc.contributor.authorNagao, Junyaja
dc.contributor.authorMiyashita, Masahiroja
dc.contributor.authorNakagawa, Yoshiakija
dc.contributor.authorMiyagawa, Hisashija
dc.contributor.alternative宮下, 正弘ja
dc.descriptionArticle first published online: 27 APR 2015ja
dc.description.abstractLa1 is a 73-residue cysteine-rich peptide isolated from the scorpion Liocheles australasiae venom. Although La1 is the most abundant peptide in the venom, its biological function remains unknown. Here, we describe a method for efficient chemical synthesis of La1 using the native chemical ligation (NCL) strategy, in which three peptide components of less than 40 residues were sequentially ligated. The peptide thioester necessary for NCL was synthesized using an aromatic N-acylurea approach with Fmoc-SPPS. After completion of sequential NCL, disulfide bond formation was carried out using a dialysis method, in which the linear peptide dissolved in an acidic solution was dialyzed against a slightly alkaline buffer to obtain correctly folded La1. Next, we determined the disulfide bonding pattern of La1. Enzymatic and chemical digests of La1 without reduction of disulfide bonds were analyzed by liquid chromatography/mass spectrometry (LC/MS), which revealed two of four disulfide bond linkages. The remaining two linkages were assigned based on MS/MS analysis of a peptide fragment containing two disulfide bonds. Consequently, the disulfide bonding pattern of La1 was found to be similar to that of a von Willebrand factor type C (VWC) domain. To our knowledge, this is the first report of the experimental determination of the disulfide bonding pattern of peptides having a single VWC domain as well as their chemical synthesis. La1 synthesized in this study will be useful for investigation of its biological role in the venom.ja
dc.rightsThis is the peer reviewed version of the following article: Nagao, J., Miyashita, M., Nakagawa, Y., and Miyagawa, H. (2015) Chemical synthesis of La1 isolated from the venom of the scorpion Liocheles australasiae and determination of its disulfide bonding pattern. J. Pept. Sci., 21: 636–643, which has been published in final form at This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.ja
dc.rightsThe full-text file will be made open to the public on 27 APR 2016 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.ja
dc.rightsThis is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。ja
dc.subjectscorpion venomja
dc.subjectpeptide synthesisja
dc.subjectnative chemical ligationja
dc.subjectdisulfide bondja
dc.titleChemical synthesis of La1 isolated from the venom of the scorpion Liocheles australasiae and determination of its disulfide bonding pattern.ja
dc.type.niitypeJournal Articleja
dc.identifier.jtitleJournal of peptide scienceja
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