Covalent and stable CuAAC modification of silicon surfaces for control of cell adhesion.
Stable primary functionalization of metal surfaces plays a significant role in reliable secondary attachment of complex functional molecules used for the interfacing of metal objects and nanomaterials with biological systems. In principle, this can be achieved through chemical reactions either in the vapor or liquid phase. In this work, we compared these two methods for oxidized silicon surfaces and thoroughly characterized the functionalization steps by tagging and fluorescence imaging. We demonstrate that the vapor-phase functionalization only provided transient surface modification that was lost on extensive washing. For stable surface modification, a liquid-phase method was developed. In this method, silicon wafers were decorated with azides, either by silanization with (3-azidopropyl)triethoxysilane or by conversion of the amine groups of an aminopropylated surface by means of the azido-transfer reaction. Subsequently, D-amino acid adhesion peptides could be immobilized on the surface by use of Cu(I)-catalyzed click chemistry. This enabled the study of cell adhesion to the metal surface. In contrast to unmodified surfaces, the peptide-modified surfaces were able to maintain cell adhesion during significant flow velocities in a microflow reactor.
Center for Evolutionary Chemical Biology, Department of Chemistry, University of Copenhagen, Universitetsparken 5, 2100 Copenhagen (Denmark).
Surendra
S
Vutti
Nina
N
Buch-Månson
Sanne
S
Schoffelen
Nicolas
N
Bovet
Karen L
KL
Martinez
Morten
M
Meldal
D000480:Alkynes / Q000737:chemistry*; D001386:Azides / Q000737:chemistry*; D002384:Catalysis; D002448:Cell Adhesion; D003300:Copper / Q000737:chemistry*; D003500:Cyclization; D005453:Fluorescence; D057809:HEK293 Cells; D006801:Humans; D015394:Molecular Structure; D012825:Silicon / Q000737:chemistry*; D013499:Surface Properties
D000480:Alkynes; D001386:Azides; D003300:Copper; D012825:Silicon
cell membrane interactions; click chemistry; fluorescence labeling; peptide immobilization; surface chemistry