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• W2023996387 abstract "Molecular systems composed of peptides or proteins can be programmed to yield intriguing and potentially useful supra-molecular architectures. In the past decade peptide self-assemblies at interfaces have been the subject of various studies aiming at formation of molecular structures with predictable patterns and properties. Most of these systems utilized amphiphilic peptides, usually of a particular secondary structure, that self-assemble through non-covalent intermolecular interactions, into two-dimensional, organized supramolecular structures. The interest in design and preparation of self-assembled functional materials is driven by potential benefits to nanotechnology and nanobiotechnology. This review is restricted to amphiphilic peptide assemblies at interfaces studied by grazing incidence X-ray diffraction and atomic force microscopy, geared towards nanometer-scale structural characterizations." @default.
• W2023996387 created "2016-06-24" @default.
• W2023996387 creator A5031010685 @default.
• W2023996387 date "2006-07-01" @default.
• W2023996387 modified "2023-09-26" @default.
• W2023996387 title "Ordered Peptide Assemblies at Interfaces" @default.
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• W2023996387 doi "https://doi.org/10.1080/10610270600665905" @default.
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