An investigation of the role of the adiponectin variable domain on the stability of the collagen-like domain

Authors

  • Paul W. R. Harris,

    1. School of Chemical Sciences, The University of Auckland, Auckland, New Zealand
    2. Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland, New Zealand
    3. Institute for Innovation in Biotechnology, The University of Auckland, Auckland, New Zealand
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  • Lutz Hampe,

    1. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
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  • Mazdak Radjainia,

    1. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
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  • Margaret A. Brimble,

    1. School of Chemical Sciences, The University of Auckland, Auckland, New Zealand
    2. Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland, New Zealand
    3. Institute for Innovation in Biotechnology, The University of Auckland, Auckland, New Zealand
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  • Alok K. Mitra

    Corresponding author
    1. Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland, New Zealand
    2. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
    • Correspondence to: Alok K. Mitra; Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Private Bag 92019, Auckland 1010, New Zealand; e-mail: a.mitra@auckland.ac.nz

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  • This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

ABSTRACT

The chemical synthesis is described of a polypeptide construct possessing both the variable and the collagen-like domain of adiponectin, which can be used as a model system for probing the influence of the variable domain on multimerization of this important circulating hormone. Using a collagen domain repeat peptide unit derived from native adiponectin or a glutamic acid analogue was ineffective due to noncollagenous conformational properties in both cases. However, employing a collagen model peptide and linking this to the variable domain thioester peptide using native chemical ligation proved effective. The 63 residue peptide was characterized by circular dichroism and mass spectrometry which demonstrated that a collagen-like triple-helical structure was preserved. © 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 313–321, 2014.

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