Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures |
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Authors: | Koga Tomoyuki Higuchi Masahiro Kinoshita Takatoshi Higashi Nobuyuki |
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Institution: | Department of Molecular Science & Technology, Faculty of Engineering, Doshisha University, Kyotanabe, Kyoto 610-0321, Japan. |
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Abstract: | Here, we report a novel, programmable, molecular self-assembling system to fabricate shape-specific, three-dimensional nanoarchitectures. Three types of simple 16-mer peptides consisting of hydrophobic Leu and hydrophilic Lys, LKL16, KLK16, and LK16, were prepared as building blocks for nanofabrications. A detailed analysis of the conformation and self-assembling mechanism was performed by using circular dichroism (CD), FTIR spectroscopy, and atomic force microscopy (AFM). A wide variety of self-assembled nanoarchitectures, such as beta-sheet-plates, beta-sheet-fibers, alpha-helix-particles, and alpha-helix-plates, could be fabricated by tuning the peptide sequence, reaction time, and solution pH. The ability to control the self-assembled nanostructures should provide a simple and/or essential insight into the mechanism of peptide aggregation, including amyloid formation, and it should be useful for the design of novel bio-related nanomaterials. |
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Keywords: | amphiphilic peptides amyloids conformation analysis nanostructures self‐assembly |
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