Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 12, Issue 5, Pages 1360-1367Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.200500611
Keywords
amphiphilic peptides; amyloids; conformation analysis; nanostructures; self-assembly
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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 (M), 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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