Remarkable progress has been made to date in the discovery of material binding peptides and their utilization in nanotechnology, which has brought new challenges and opportunities. Nowadays phage display is a versatile tool which has been adapted over the past decade to select material-specific peptides. Screening and selection of such phage displayed material binding peptides has attracted great interest, in particular because of their use in nanotechnology. Phage display selected peptides are either synthesized independently or expressed on phage coat protein. Selected phage particles are subsequently utilized in the synthesis of nanoparticles, in the assembly of nanostructures on inorganic surfaces, and oriented protein immobilization as fusion partners of proteins. The use of proteins to build artificial supramolecular nanostructures has advanced with the development of a computational method to design peptides that will self-organize into specific supramolecular structures on a given surface. Specifically, peptides that assemble on the surface of carbon nanotubes have been designed. Engineering structures on the smallest possible scales — using molecules and individual atoms as building blocks — is both physically and conceptually challenging. Recently, a method of computationally selecting the best of these blocks, drawing inspiration from the similar behavior of proteins in making biological structures has been developed. Proteins that can wrap around single-walled carbon nanotubes have been achieved. An algorithm that sifts through hundreds of thousands of atomically detailed actual and potential protein structures has been designed and can be compared with the structural parameters of the desired scaffolding. This algorithm can be used to design a protein that would not only stably wrap around a nanotube in a helix but also provide a regular pattern on its exterior to which gold particles could be attached. In this paper, we present an overview on the research conducted on this area.