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Biophysical characterization of recombinant human ameloblastin

Authors

  • Tomáš Wald,

    1. Institute of Microbiology v.v.i, Academy of Sciences of the Czech Republic, Vídeňská, 1083, 142 20 Prague 4 Czech Republic
    2. Institute of Chemical Technology, Prague 6, Czech Republic
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  • Lucie Bednárová,

    1. Institute of Organic Chemistry and Biochemistry v.v.i., Academy of Sciences of the Czech Republic, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic
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  • Radim Osička,

    1. Institute of Microbiology v.v.i, Academy of Sciences of the Czech Republic, Vídeňská, 1083, 142 20 Prague 4 Czech Republic
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  • Petr Pachl,

    1. Institute of Organic Chemistry and Biochemistry v.v.i., Academy of Sciences of the Czech Republic, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic
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  • Miroslav Šulc,

    1. Institute of Microbiology v.v.i, Academy of Sciences of the Czech Republic, Vídeňská, 1083, 142 20 Prague 4 Czech Republic
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  • Stale Petter Lyngstadaas,

    1. Department of Biomaterials, University of Oslo, Oslo, Norway
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  • Ivan Slaby,

    1. Institute of Biotechnology v.v.i., Academy of Sciences of the Czech Republic, Vídeňská 1083, 142 00 Prague 4, Czech Republic
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  • Jiří Vondrášek

    1. Institute of Organic Chemistry and Biochemistry v.v.i., Academy of Sciences of the Czech Republic, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic
    2. Institute of Biotechnology v.v.i., Academy of Sciences of the Czech Republic, Vídeňská 1083, 142 00 Prague 4, Czech Republic
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Jiri Vondrasek, Institute of Biotechnology v.v.i., Academy of Sciences of the Czech Republic, Vídeňská 1083, 142 20 Prague 4, Czech Republic

Telefax: +420–244–472282
E-mail: jiri.vondrasek@img.cas.cz

Abstract

Wald T, Bednárová L, Osička R, Pachl P, Šulc M, Lyngstadaas SP, Slaby I, Vondrášek J. Biophysical characterization of recombinant human ameloblastin.
Eur J Oral Sci 2011; 119 (Suppl. 1): 261–269. © 2011 Eur J Oral Sci

Ameloblastin (AMBN) is a protein expressed mainly during dental hard tissue development. Biochemically, it is classified as an intrinsically disordered protein (IDP). Its biological role remains largely unknown; however, the question of AMBN function will undoubtedly be connected to its structural properties and its potential for protein–protein and protein–cell interactions. A basic biophysical characterization of human recombinant ameloblastin (hrAMBN) and its N- and C-terminal domains by means of circular dichroism spectroscopy and dynamic light scattering showed that under physiological conditions ameloblastin is an IDP with a prevalent polyproline-II (PPII) conformation. Both the N- and C-terminal polypeptides, when expressed independently, showed different structural preferences upon heating as well as different behaviour in the presence of trifluoroethanol and CaCl2 salt. The N-terminal peptide showed a more ordered structure with a strong tendency to adopt a helical conformation upon the addition of trifluorethanol, whereas the C-terminal domain seemed to be primarily responsible for the structural disorder of the entire AMBN molecule.

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