Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly

• Published in: Nature (London) Vol. 405; no. 6787; pp. 665 - 668
• Main Authors: Belcher, Angela M, Whaley, Sandra R, English, D. S, Hu, Evelyn L, Barbara, Paul F
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 08.06.2000; Nature Publishing Group
• Subjects: Amino Acid Sequence; Amino acids; Bacteriophage M13; Biological and medical sciences; Calcium carbonate; Capsid Proteins; Crystalline structure; DNA-Binding Proteins - analysis; DNA-Binding Proteins - metabolism; Fabrication; Fundamental and applied biological sciences. Psychology; Microscopy, Atomic Force; Microscopy, Fluorescence; Molecular biophysics; Nucleation; Optical properties; Peptide Library; Peptides; Peptides - analysis; Peptides - metabolism; Protein Binding; Proteins; Semiconductors; Silica; Structure in molecular biology; Viral Fusion Proteins - analysis; Viral Fusion Proteins - metabolism; Semiconductor materials; Peptides; Chemical bond; Joining; Crystallography; X ray diffraction; Nanocrystal; Aminoacid sequence; Crystalline structure; Biological system
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/35015043

In biological systems, organic molecules exert a remarkable level of control over the nucleation and mineral phase of inorganic materials such as calcium carbonate and silica, and over the assembly of crystallites and other nanoscale building blocks into complex structures required for biological function. This ability to direct the assembly of nanoscale components into controlled and sophisticated structures has motivated intense efforts to develop assembly methods that mimic or exploit the recognition capabilities and interactions found in biological systems. Of particular value would be methods that could be applied to materials with interesting electronic or optical properties, but natural evolution has not selected for interactions between biomolecules and such materials. However, peptides with limited selectivity for binding to metal surfaces and metal oxide surfaces have been successfully selected. Here we extend this approach and show that combinatorial phage-display libraries can be used to evolve peptides that bind to a range of semiconductor surfaces with high specificity, depending on the crystallographic orientation and composition of the structurally similar materials we have used. As electronic devices contain structurally related materials in close proximity, such peptides may find use for the controlled placement and assembly of a variety of practically important materials, thus broadening the scope for 'bottom-up' fabrication approaches.