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Publication:
Biofunctionalization of materials for implants using engineered peptides

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Elsevier BV

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Abstract

Uncontrolled interactions between synthetic materials and human tissues are a major concern for implants and tissue engineering. The most successful approaches to circumvent this issue involve the modification of the implant or scaffold surfaces with various functional molecules, such as anti-fouling polymers or cell growth factors. To date, such techniques have relied on surface immobilization methods that are often applicable only to a limited range of materials and require the presence of specific functional groups, synthetic pathways or biologically hostile environments. In this study we have used peptide motifs that have been selected to bind to gold, platinum, glass and titanium to modify surfaces with poly(ethylene glycol) anti-fouling polymer and the integrin-binding RGD sequence. The peptides have several advantages over conventional molecular immobilization techniques; they require no biologically hostile environments to bind, are specific to their substrates and could be adapted to carry various active entities. We successfully imparted cell-resistant properties to gold and platinum surfaces using gold- and platinum-binding peptides, respectively, in conjunction with PEG. We also induced a several-fold increase in the number and spreading of fibroblast cells on glass and titanium surfaces using quartz and titanium-binding peptides in conjunction with the integrin ligand RGD. The results presented here indicate that control over the extent of cell-material interactions can be achieved by relatively simple and biocompatible surface modification procedures using inorganic binding peptides as linker molecules.

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Acta Biomaterialia

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1742-7061

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CLOSED

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Titanium, Phalloidine, Surface Properties, Molecular Sequence Data, Water, Biocompatible Materials, Prostheses and Implants, Microscopy, Atomic Force, Protein Engineering, Mice, Microscopy, Fluorescence, Cell Adhesion, NIH 3T3 Cells, Animals, Humans, Amino Acid Sequence, Gold, Peptides

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