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Published May 17, 2004 | Supplemental Material
Journal Article Open

Parallel β-Sheet Assemblies at Interfaces

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 b-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 β-sheet ordered assemblies at interfaces by using strands programmed to adopt distinct intermolecular electrostatic interactions.

Additional Information

© 2004 Wiley-VCHV erlag GmbH& Co. KGaA, Weinheim Received: November 7, 2003 [Z1046] This work was supported by the United States-Israel Binational Science Foundation (Grant No. 2001149) and by the IHP-Contract HPRI-CT-2001±00140 of the European Commission. We acknowledge HASYLAB for synchrotron beamtime. We thank Leslie Leiserowitz for helpful discussions, Inna Solomonov for synchrotron measurements, Mark Karpasas for MALDI measurements, and Vitaly Yerochimovich for help with the FTIR work.

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