Predictably interfacing biological molecules with solids is the key for drug delivery, enzyme immobilization, biofunctionalization of implants, and signal transduction in biosensors. Highly specific interactions controlled by proteins enable explicit recognition of minerals and formation of intricate supramolecular architectures in nature. Mimicking natural proteins, engineered short polypeptides have become ubiquitous molecular tools in addressable functionalization of solid interfaces. Simplicity of peptide sequences and functional domains offer latent means for tailoring and interrogating intermolecular forces through rational mutations. Direct experimental observation of interaction of peptides with solids requires well-defined surfaces, e.g., atomic-scale topography, crystal structure, or surface chemistry, kept persistent under biological conditions. These requirements are realized with metals (Au), 2D solids, e.g., graphene and layered dichalcogenides, and Quartz. Using designed or biocombinatorially selected peptides, we demonstrate control of molecular interactions on surfaces leading to organized architectures, used in technological implementations in FET devices, LEDs, remineralization and biomimetic PVs.