Many researchers have studied in vivo combinatorial biotechnology, e.g., either phage or cell-surface display techniques, and developed polypeptide sequences, which can specifically bind to metals [5] [6] [7] , oxides [8, 9] , and semiconductors [10] [11] [12] . Among them, gold-binding polypeptide (GBP) is one of the genetically engineered proteins for a strong binding onto the gold surface [7, 13, 14] . Whereas many proteins and chemicals bind to the gold surface with thiol linkage, GBP does not contain a cysteine residue having thiol group. Although the definite mechanism is not clear yet, it is estimated that these polar groups in GBPs seem to coordinately interact with the gold surface within a monolayer [15, 16] . In addition, the kinetics and thermodynamics of biomimetic interactions between the GBP, and the gold surface were investigated by surface plasmon resonance (SPR) [14, 17, 18] . Compared with other thiol-based systems, the GBP binds tightly to the gold surface due to the lower standard Gibbs free energy for the bond, and the binding process is fast under aqueous conditions compatible with biological environments [14, 17, 19] . These characteristics suggest its potential applications in nano-and bio-technologies as novel agents for surface functionalization [13] .