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F. B. Wiedemann-Bidlack, E. Beniash, Y. Yamakoshi, J. P. Simmer, H. C. Margolis, “pH triggered self-assembly of native and recombinant amelogenins under physiological pH and temperature in vitro,” J Struct Biol, Vol. 160:, 2007, pp. 57-69.

has been cited by the following article:

• TITLE: Unbinding Process of Amelogenin and Fibrinogen Adsorbed on Different Solid Surfaces Using AFM

  AUTHORS: Ludovic Richert, Abdessamad Boukari, Simon Berner, Michel Dard, Joseph Hemmerlé

  KEYWORDS: Amelogenin, Titanium, Calcium phosphate; Force-mode AFM

  JOURNAL NAME: Journal of Biomaterials and Nanobiotechnology, Vol.2 No.3, May 20, 2011

  ABSTRACT: The interaction of proteins with solid surfaces is a fundamental phenomenon in the biomaterials field. We investigated, using atomic force microscopy (AFM), the interactions of a recombinant amelogenin with titanium, a biphasic calcium phosphate (BCP) and mica. The unbinding processes were compared to those of an earlier studied protein, namely fibrinogen. Force spectroscopy (AFM) experiments were carried out at 0 ms, 102 ms, 103 ms and 104 ms of contact time. In general, the rupture forces increased as a function of interaction time. The unbinding forces of amelogenin interacting with the BCP surface were always stronger than those of the amelogenin-titanium system. The unbinding forces of fibrinogen interacting with the BCP surface were always much stronger than those of the fibrinogen-titanium system. For the most part, this study provides direct evidence that recombinant amelogenin binds more strongly than fibrinogen on the studied substrates.