Parallel β-Sheet Assemblies at Interfaces Academic Article uri icon

abstract

  • Polypeptide assemblies may exhibit various topologies [1±9] that are of interest for nanometer-scale surface patterning and its potential applications. The success in designing such ordered molecular architectures entails control over peptide conformations and intermolecular interactions. At the air±water interface peptides composed of alternating hydrophilic and hydrophobic amino acids tend to adopt β-sheet structures [10] yet the repetitive nature of these peptides also promotes nonspecific intermolecular aggregation. Recently, in several systems of de novo designed β-sheet peptides two-dimensional order has been demonstrated by grazing incidence X-ray diffraction [8, 9] and by scanning probe microscopy;[11] the extent of molecular registry has been associated with peptide composition and molecular chain length. Here we aim at formation of parallel βsheet …

publication date

  • May 17, 2004