Biocompatible Silicon Surfaces through Orthogonal Click Chemistries and a High Affinity Silicon Oxide Binding Peptide

http://pubs.acs.org/doi/full/10.1021/bc3003875

The authors used a silicon oxide binding peptide with orthogonal conjugation sites to attach a cell adhesion site and a fluorescent tag to glass surfaces. They synthesized the minimal binding sequence from a known silicon oxide binding peptide using solid phase peptide synthesis. On the ends of this peptide they incorporated an alkyne and a tetrazine ligand. They conjugate a cyclic RGD-norbornene to the tetrazine and a TAMRA-azide. Conjugation reactions could not be performed simultaneously, probably due to complexation of the copper with the tetrazine leading to inhibition of the inverse-electron demand Diels-Alder. The peptide showed high binding for the SiO2 surface with good stability and high coverage of the surface. Cell adhesion and coverage was also high.