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Protein adsorption on detonation nanodiamond/polymer composite layers

Authors
Publication Date
Keywords
  • Qc Physics / Fizika
  • Qh3020 Biophysics / Biofizika
Disciplines
  • Biology
  • Chemistry

Abstract

Composite layers of the detonation nanodiamond/polymer type possess a spatial organization of components with new structural features and physical properties, as well as complex functions due to the strong synergistic effects between the nanoparticles and polymer [1]. Composite layers were deposited by a plasma polymerization (PP) process of the detonation nanodiamond (DND) particles added to a hexamethyl disiloxan (HMDS) monomer [1]. The incorporation of silver ions in the polymer leads to the production of materials that are highly efficient against bacterial colonization and allows better cell adhesion and spreading. [2] For cell culture processes, fibronectin (FN) treatment is one of the commonly used approaches to enhance the cell adhesion on a surface [3]. As an integrated part of our search for improved materials for life science applications such as biomaterials and biosensors, the objective of the present study is to investigate the interaction of Ag-based composite surfaces with FN protein. Two types of composite layers, Ag-ND/PPHMDS and Ag-nano/PPHMDS were obtained by plasma polymerization of HMDS and nanoparticles of Ag and Ag-DND. The composite layers are representative of the different incorporation of the Ag in the polymer net. The structures studied, consisting of composite layers with adsorbed FN were optically characterized with Ellipsometry, Fourier Transform Infrared (FTIR) and Ultra Violet (UV) Spectroscopy as well as by stylus profiling (Talysurf). The kinetic study of the FN adsorption indicates that the process depends on the FN concentration and the exposure time as well as on the surface chemistry of the composites. Compared to the reference sample, all composite layers exhibit an indication of a stronger ability to initiate the intrinsic pathway of coagulation. © 2012 Materials Research Society.

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