ABSTRACTCombinatorial phage display with a pVIII library of M13 bacteriophage was used to identify a peptide sequence capable of recognition and mineralization of copper sulfide. The six sequences isolated from the final biopanning round were rich in basic, hydrophobic, and polar amino acids compared to the phage display library. The peptide sequence, DTRAPEIV, was used to biomineralize copper sulfide on the pVIII major coat protein thus producing linear chains of nanoparticles. Electron microscopy revealed that the phage was capable of controlling the size of the nucleated nanoparticles in an aqueous solution at room temperature and that the mineralized material was copper sulfide. Phage-templated biomineralization is a low temperature, aqueous-based approach to synthesis of copper sulfide nanoparticles with hierarchical order.