Direct and reversible immobilization and microcontact printing of functional proteins on glass using a genetically appended silica-binding tag.

Fusion of disulfide-constrained or linear versions of the Car9 dodecapeptide to model fluorescent proteins support their on-contact and oriented immobilization onto unmodified glass. Bound proteins can be released and the surface regenerated by incubation with l-lysine. This noncovalent chemistry enables rapid and reversibe microcontact printing of tagged proteins and speeds up the production of bicontinuous protein patterns.