Article citationsMore>>

J. Svensson. C. Andersson., J. E. Reseland, P. Lyngstadaas, L. Bülow, “Histidine tag fusion increases expression levels of active recombinant amelogenin in Escherichia coli,” Protein Expr Purif, Vol. 48, 2006, pp. 134-141.

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.