Fibrinogen Patterns and Activity on Substrates with Tailored Hydroxy Density

• Published in: Macromolecular bioscience Vol. 9; no. 8; pp. 766 - 775
• Main Authors: Rodríguez Hernández, José Carlos, Rico, Patricia, Moratal, David, Monleón Pradas, Manuel, Salmerón-Sánchez, Manuel
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 11.08.2009; WILEY‐VCH Verlag; Wiley-VCH
• Subjects: 3T3 Cells; Acrylates - chemistry; Adsorption; Animals; Applied sciences; Atomic force microscopy; Biocompatible Materials; Biological and medical sciences; Biomimetic Materials - chemistry; Cell Adhesion; cell-material interaction; Density; Exact sciences and technology; Fibrinogen; Fibrinogen - chemistry; Fractal analysis; Fundamental and applied biological sciences. Psychology; Hydrophobic and Hydrophilic Interactions; Image analysis; Mice; Microscopy, Atomic Force; Molecular biophysics; Organic polymers; Physicochemistry of polymers; Polymers - chemistry; Properties and characterization; proteins; Solution and gel properties; Surface chemistry; Surface Properties; Surface properties. Adsorption; Thrombin; Wettability; Liquid solid adsorption; Adsorption capacity; Experimental study; Protein; Biological activity; Colloidal gel; Wettability; Cell adhesion; Adsorbed state; Fibrinogen; Surface properties; Ethyl acrylate copolymer; Hydroxyethyl acrylate copolymer; Fibroblast; Conformation
• ISSN: 1616-5187; 1616-5195
• DOI: 10.1002/mabi.200800332

The influence of the surface fraction of OH groups on fibrinogen (FG) adsorption is investigated in copolymers of ethyl acrylate and hydroxy ethylacrylate. The amount of adsorbed FG, quantified by western‐blotting combined with image analysis of the corresponding bands, decreases as the hydrophilicity of the substrate increases. The influence of substrate wettability on FG conformation and distribution is observed by atomic force microscopy (AFM). The most hydrophobic substrate promotes FG fibrillogenesis, which leads to a fibrin‐like appearance in the absence of any thrombin. The degree of FG interconnection was quantified by calculating the fractal dimension of the adsorbed protein from image analysis of the AFM results. The biological activity of the adsorbed FG is correlated to cell adhesion on FG‐coated substrates. Fibrinogen adsorption on model substrates with controlled OH density is quantified by western‐blotting and its conformation directly observed by AFM. Substrate‐induced fibrinogen fibrillogenesis is enhanced on some substrates as a consequence of protein material interactions, in absence of either any thrombin or cells. The protein conformation is related to initial cell adhesion.