1. Facile and efficient assembly of collagen-like triple helices on a TRIS scaffold
- Author
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Cai, Weibo, Wong, Dustin, Kinberger, Garth A., Kwok, Sen Wai, Taulane, Joseph P., and Goodman, Murray
- Subjects
- *
CONNECTIVE tissues , *EXTRACELLULAR matrix proteins , *COLLAGEN , *OPTICAL polarization - Abstract
Abstract: The TRIS scaffold, Boc-β-Ala-TRIS-(OH)3, was utilized to assemble triple helices composed of the Gly-Nleu-Pro sequence (Nleu denotes N-isobutylglycine). The scaffold assembly can be achieved efficiently through direct coupling between long peptide chains and the TRIS scaffold using DEPBT, a recently developed peptide coupling reagent. CD spectroscopy and thermal denaturation studies demonstrated that Boc-β-Ala-TRIS-[(Gly-Nleu-Pro) n -OMe]3 exhibits triple helicity in H2O when n equals 5, 6, and 8, while the shorter analogs (where n =1 and 4) do not. TRIS-assembled structures possess several advantages over the KTA- and TREN-assembled structures previously reported from our laboratory (where KTA and TREN denotes cis-1,3,5-trimethyl cyclohexane-1,3,5-tricarboxylic acid and tris(2-aminoethyl)amine, respectively). The protecting groups on the scaffold and at the C-terminus of the TRIS-assembled peptides can be readily removed to synthesize collagen mimetic dendrimers and metal-complexing collagen-like peptides respectively, both of which can lead to further enhanced thermal stability. [Copyright &y& Elsevier]
- Published
- 2007
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