Biophysical characterization of recombinant human ameloblastin

0390090 - MBÚ 2013 RIV US eng J - Journal Article
Wald, Tomáš - Bednárová, Lucie - Osička, Radim - Pachl, Petr - Šulc, Miroslav - Lyngstadaas, S. P. - Slabý, Ivan - Vondrášek, Jiří
Biophysical characterization of recombinant human ameloblastin.
European Journal of Oral Sciences. Roč. 119, č. 1 (2011), s. 261-269. ISSN 0909-8836. E-ISSN 1600-0722
R&D Projects: GA ČR GAP302/10/0427; GA MŠMT LC512
Keywords : circular dichroism spectroscopy * dynamic light scattering * enamel matrix protein
Subject RIV: EE - Microbiology, Virology
Impact factor: 1.878, year: 2011

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 CaCl(2) 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
Permanent Link: http://hdl.handle.net/11104/0219039