Comparison between RGD-peptide-modified titanium and borosilicate surfaces |
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Authors: | N?Senyah G?Hildebrand Email author" target="_blank">K?LiefeithEmail author |
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Institution: | (1) Department of Biomaterials, Institute for Bioprocessing and Analytical Measurement Techniques e.V. (iba), Rosenhof, 37308 Heilbad Heiligenstadt, Germany |
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Abstract: | The use of synthetic peptides containing adhesive sequences, such as the Arg-Gly-Asp (RGD) motif, represents a promising strategy
to control biological interactions at the cell–material interface. These peptides are known to improve the tissue–material
contact owing to highly specific binding to cellular membrane receptors known as integrins, thereby promoting the adhesion,
migration and proliferation of cells. The peptides were coupled to borosilicate glass and titanium surfaces using silanisation
chemistry. A tryptophan residue was incorporated into the amino acid sequences of selected peptides to facilitate the detection
of the covalently bound peptides. Successful peptide immobilisation was proven by fluorimetric measurements. The confocal
imaging analysis suggests a homogeneous distribution of the immobilised peptide across the biomaterial surface. In vitro cell
proliferation assays were employed to compare the adhesion potentials of the well-known RGD-containing peptides GRGDSP, GRADSP
and RGDS to the three peptides designed by our group. The results demonstrate that the RGD sequence is not necessarily required
to enhance the adhesion of cells to non-biological surfaces. Moreover, it is shown that the number of adhering cells can be
increased by changes in the peptide hydrophobicity. Changes in the cytoskeleton are observed depending on the type of RGD-peptide
modification. |
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Keywords: | RGD-peptides Surface distribution Cell adhesion Osteoblasts Titanium |
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