Abstract
Self-assembly of small molecules into highly ordered nanostructures offers many important potential applications in science research and industry. Precise self-assembling with the assistance of inorganic substrate is considered as an ideal strategy. In this experiment, the highly ordered mica surface was used to template the assembling of a novel designed amphiphilic hexapeptide to form orderly parallel fibers. The nanostructure and the self-assembly mechanism were investigated by atomic force microscopy (AFM), transmission electron microscopy, Fourier transform infrared spectroscopy, and circular dichroism techniques. By the experimental results, a dramatic conformation transition from random coil and/or α-helix into β-sheet was found after the peptide assembled on the mica surface under certain conditions, which was considered as a key factor for the ordered nanostructure. Finally, according to the AFM images and the simulated length of peptide molecules, a trilaminar β-sheet structure model was proposed to explain the hierarchical self-assembly mechanism.
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Acknowledgments
This work is supported by the research project of Sichuan Education Office (10ZC091), the Fundamental Research Funds for the Central Universities (12NZYQN11), and Natural Science Foundation of the Chengdu Medical College (CYZ11-010).
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Lin, J., Luo, JB., Yang, ST. et al. Template-directed self-assembly of a designed amphiphilic hexapeptide on mica surface. Colloid Polym Sci 291, 2263–2270 (2013). https://doi.org/10.1007/s00396-013-2969-y
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DOI: https://doi.org/10.1007/s00396-013-2969-y