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A comparison of three- and four-helix bundle TASP molecules

TitleA comparison of three- and four-helix bundle TASP molecules
Publication TypeJournal Article
Year of Publication2002
AuthorsCauston, AS, Sherman, JC
JournalJournal of Peptide Science
Volume8
Pagination275-282
Date PublishedJun
Type of ArticleArticle
ISBN Number1075-2617
Keywords4-HELIX BUNDLES, DESIGN, four-helix bundle, PROTEIN, STABILITY, TASP, template assembled synthetic protein, three-helix bundle
Abstract

We have designed, synthesized and characterized three- and four-helix bundle template-assembled synthetic proteins (TASPs). The TASPs were synthesized using disulphide bonds between the peptides and either the cyclotribenzylene (CTB) template, or the cavitand (BOWL) template, to form the three- and four helix bundles, respectively. The TASPs were constructed using peptides that were linked via their N-termini (peptide CGGGEELLKKXEELLKKG, where X = L, I, Nle or V), or via their C-termini (peptide GEELLKKLEELLKKGGGC). Each TASP was assayed for its structure, stability, ’native-like’ characteristics and whether it was a monomer in solution. All TASPs were found to be highly helical, and highly resistant to chemical denaturation using guanidine hydrochloride (GnHCl). Analysis of the GnHCl-induced unfolding curves of the different TASPs demonstrated stability differences based on the number of helices in the bundle, the end of the helix that was attached to the template, and the identity of the core amino acid. The TASPs all had molten-globule structure, which is (generally) consistent with a degenerate sequence in the core. The four-helix bundle TASPs appeared to be monomers in solution, whereas there is some evidence that the three-helix bundle TASPs are weakly self associating. Copyright. (C) 2002 European Peptide Society and John Wiley Sons, Ltd.

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