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Bioconjug Chem. 2012 Oct 17;23(10):2129-37. doi: 10.1021/bc3003875. Epub 2012 Sep 27.

Biocompatible silicon surfaces through orthogonal click chemistries and a high affinity silicon oxide binding peptide.

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Institut für Biochemie, Faculty of Biosciences, Pharmacy and Psychology, Universität Leipzig, Brüderstrasse 34, 04103 Leipzig, Germany.


Multifunctionality is gaining more and more importance in the field of improved biomaterials. Especially peptides feature a broad chemical variability and are versatile mediators between inorganic surfaces and living cells. Here, we synthesized a unique peptide that binds to SiO(2) with nM affinity. We equipped the peptide with the bioactive integrin binding c[RGDfK]-ligand and a fluorescent probe by stepwise Diels-Alder reaction with inverse electron demand and copper(I) catalyzed azide-alkyne cycloaddition. For the first time, we report the generation of a multifunctional peptide by combining these innovative coupling reactions. The resulting peptide displayed an outstanding binding to silicon oxide and induced a significant increase in cell spreading and cell viability of osteoblasts on the oxidized silicon surface.

[Indexed for MEDLINE]

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