A general approach to immobilize proteins regio- and chemoselectively to gold surfaces using protein farnesyltransferase

A general strategy for immobilizing soluble proteins regio- and chemoselectively to surfaces through an unnatural amino acid generated by post-translational modification of a cysteine residue by Protein Farnesyltransferase to gold surfaces is described. We successfully introduce azide and alkyne functional groups into the carboxyl-terminus of natively folded proteins and covalently attach them to monolayers bearing complementary functional groups on gold slides and nanoparticles. The structural integrity of the immobilized proteins was retained.