Antibodies are affinity proteins with a wide spectrum of applications in analytical and therapeutic biology. Proteins showing specific recognition for a chosen molecular target can be isolated and their encoding sequence identified in vitro from a large and diverse library by phage display selection. In this work, we show that this standard biochemical technique rapidly yields a collection of antibody protein binders for an inorganic target of major technological importance: crystalline metallic gold surfaces. 21 distinct anti-gold antibody proteins emerged from a large random library of antibodies and were sequenced. The systematic statistical analysis of all the protein sequences reveals a strong occurrence of arginine in anti-gold antibodies, which corroborates recent molecular dynamics predictions on the crucial role of arginine in protein/gold interactions. Once tethered to small gold nanoparticles using histidine tag chemistry, the selected antibodies could drive the self-assembly of the colloids onto the surface of single crystalline gold platelets as a first step towards programmable protein-driven construction of complex plasmonic architectures. Electrodynamic simulations based on the Green Dyadic Method suggest that the antibody-driven assembly demonstrated here could be exploited to significantly modify the plasmonic modal properties of the gold platelets. Our work shows that molecular biology tools can be used to design the interaction between fully folded proteins and inorganic surfaces with potential applications in the bottom-up construction of plasmonic hybrid nanomaterials.