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

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, 10 2 ms, 10 3 ms and 10 4 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.

Computational Characterization of Mechanical, Hemodynamic, and Surface Interaction Conditions: Role of Protein Adsorption on the Regenerative Response of TEVGs

“…In fact, our multiphysics fully coupled model indicates similar time-dependent surface saturation levels compared with those reported by Manzi et al [32] as evidenced by albumin saturation after about 1.5 s. Results reported by Richert, et al [33] show that fibrinogen adsorption saturation time occurs around 1 s. Altogether, these results suggest that protein adsorption kinetics for short times can be modeled with relatively high accuracy by coupling a mutiphysic model with a two-way FSI model. This prediction capacity is important because most relevant protein adsorption events defining success or failure occur during the first seconds after blood interaction under pulsatile flow.…”

Atomic force microscopy in biomaterials surface science

“…For example, single-molecule force spectroscopy quantified via force-distance curves protein unraveling, folding and unfolding mechanisms, receptor-ligand and ligandbinding interactions. 53,74,75 Research aiming at characterizing protein-biomaterials interactions can capitalize on these and similar studies 76 and determine how nanometric surface cues affect parameters of protein adsorption such as adhesion and unbinding forces. The capacity of SMFS to probe molecular events can also be exploited to investigate the interactions and the dynamics of a variety of cell-surface-associated proteins.…”

“…contact time). 76 In this context, various groups have been exploring the controlled delivery of viral vectors to overcome some of the current challenges in gene therapy and tissue engineering by improving site targeting, reducing inflammatory and immune responses, enhancing transduction and extending the duration of gene expression. 82 Recently, strategies for specific vector-biomaterial binding based on the interactions of functional groups on viral capsid and functionalized surfaces (e.g.…”