Monodispersed Dimerization of Isoleucine Zipper–Coiled Coil Trimer

We describe the synthesis and characterization of novel isoleucine zipper polypeptide dimers, connected with a maleimide-containing linker molecule, that can assemble into structurally defined heterotrimeric α-helical coiled coil dimers on the basis of architectural features of the polypeptide seque...

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Bibliographic Details
Published in:Bulletin of the Chemical Society of Japan 2007-07, Vol.80 (7), p.1296-1301
Main Authors: Kashiwada, Ayumi, Sakakibara, Atsuko, Nakamura, Yohei, Matsuda, Kiyomi
Format: Article
Language:English
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Summary:We describe the synthesis and characterization of novel isoleucine zipper polypeptide dimers, connected with a maleimide-containing linker molecule, that can assemble into structurally defined heterotrimeric α-helical coiled coil dimers on the basis of architectural features of the polypeptide sequences. Linear- and crosslinked-isoleucine zipper polypeptide dimers were designed in this study. Circular dichroism spectroscopy, gel filtration, and HPLC analyses indicate that each polypeptide dimer can noncovalently assemble with four isoleucine zipper polypeptides and lead to heterotrimeric α-helical coiled coil dimer formation. Thus, we concluded that monodispersed dimerization of triple-stranded coiled coil was achieved for the first time. Moreover, the noncovalently assembled supramolecule may be useful as a the building-block for constructing artificial polypeptide fibrillogenesis systems.
ISSN:0009-2673
1348-0634
DOI:10.1246/bcsj.80.1296