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Adsorption-induced fibronectin aggregation and fibrillogenesis.
Delphine Pellenc1, Hugues Berry, Olivier Gallet
1ERRMECe, Université de Cergy-Pontoise, 2 avenue Adolphe Chauvin BP 222, 95302 Pontoise cedex, France. delphine.pellenc@bio.u-cergy.fr
Journal of Colloid and Interface Science
|December 27, 2005
Summary
Fibronectin (Fn) self-assembly on hydroxyapatite (HA) forms fibrils and networks. This process is influenced by concentration, ionic strength, and surfactants, revealing complex fibrillogenesis mechanisms.
Area of Science:
- Biochemistry
- Materials Science
- Biophysics
Background:
- Fibronectin (Fn) is a key glycoprotein in extracellular matrix architecture, crucial for cell processes.
- The influence of mineral surfaces on fibronectin supramolecular assembly, particularly in bone biology, remains poorly understood.
Purpose of the Study:
- To investigate the morphological properties of fibronectin induced by its adsorption onto a model hydroxyapatite (HA) mineral surface.
- To elucidate the mechanisms governing fibronectin self-assembly and fibrillogenesis on HA.
Main Methods:
- Studied fibronectin adsorption onto hydroxyapatite (HA) under varying conditions (concentration, ionic strength, surfactant presence).
- Analyzed fibronectin aggregation and fibrillation using techniques including thioflavine T staining.
- Proposed a model for fibronectin fibrillogenesis on HA.
Main Results:
- Fibronectin adsorption onto HA spontaneously induces aggregation and fibrillation, forming dense networks.
- Self-assembly is time-dependent and sensitive to bulk concentration and ionic strength.
- Non-ionic surfactants promote aggregation over fibrillation; fibrils show partial amyloid-like structure.
Conclusions:
- Fibronectin self-assembly on HA involves multiple organization routes.
- The N-terminal domain has limited inhibitory effect on self-assembly.
- A model for fibronectin fibrillogenesis on hydroxyapatite is proposed, considering protein conformation and interactions.