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.