Wald Tomáš, Bednárová Lucie, Osička Radim, Pachl Petr, Sulc Miroslav, Lyngstadaas Stale Petter, Slaby Ivan, Vondrášek Jiří
Institute of Microbiology v.v.i, Academy of Sciences of Czech Republic, Vídeňská, 1083, 142 20 Prague 4 Czech Republic.
Eur J Oral Sci. 2011 Dec;119 Suppl 1:261-9. doi: 10.1111/j.1600-0722.2011.00913.x.
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.
成釉蛋白（AMBN）是一种主要在牙齿硬组织发育过程中表达的蛋白质。从生物化学角度来看，它被归类为一种内在无序蛋白质（IDP）。其生物学作用在很大程度上仍然未知；然而，AMBN的功能问题无疑将与其结构特性以及蛋白质 - 蛋白质和蛋白质 - 细胞相互作用的潜力相关联。通过圆二色光谱和动态光散射对人重组成釉蛋白（hrAMBN）及其N端和C端结构域进行的基本生物物理表征表明，在生理条件下，成釉蛋白是一种具有普遍多聚脯氨酸II（PPII）构象的IDP。当N端和C端多肽独立表达时，它们在加热时表现出不同的结构偏好，并且在三氟乙醇和CaCl₂盐存在下表现出不同的行为。N端肽在添加三氟乙醇后显示出更有序的结构，并且强烈倾向于采用螺旋构象，而C端结构域似乎是整个AMBN分子结构无序的主要原因。
