Berlin 2008 – scientific programme

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BP: Fachverband Biologische Physik

BP 26: Posters II

BP 26.12: Poster

Thursday, February 28, 2008, 17:00–19:30, Poster A

The influence of pH and temperature on the self-assembly of amelogenin and its relevance for the biomineralization of enamel — •C. Gilow¹, B. Aichmayer¹, F.B. Wiedemann-Bidlack², H.C. Margolis², and P. Fratzl¹ — ¹Max Planck Institute of Colloids and Interfaces, D-14424 Potsdam, Germany — ²The Forsyth Institute, Boston, MA 02115-3782, USA

In the early stages of dental enamel formation, amelogenin is the most abundant matrix protein. The self-assembly of amelogenin to so-called "nanospheres" is believed to control the growth and alignment of hydroxyapatite crystals in the developing enamel tissue. Previous studies [1] on the formation of these "nanospheres" and their subsequent temperature-induced aggregation showed that the interaction between the "nanospheres" is controlled by the hydrophilic C-terminus of the protein. Further studies by Wiedemann-Bidlack et al. [2] revealed that the pH-value is the dominant parameter which regulates the higher-order assembly of amelogenins. In the current study measurements with small-angle X-ray and neutron scattering techniques are used to elucidate the structure of these protein agglomerates, which - in spite of their commonly used name were found to strongly deviate from a spherical shape. Through a systematic study of the effects of temperature and pH as well as a more detailed characterisation of the shape of the "nanospheres" we hope to get a clearer understanding of the processes involved in the mineralization of dental enamel.

1.Aichmayer, B., et al., J Struct Biol, 2005. 151: 239.

2.Wiedemann-Bidlack, F.B., et al., J Struct Biol, 2007. 160: 57.