title: Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures.
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.
authors.affiliation: Department of Molecular Science & Technology, Faculty of Engineering, Doshisha University, Kyotanabe, Kyoto 610-0321, Japan.
authors.forename: Tomoyuki
authors.initials: T
authors.lastname: Koga
authors.forename: Masahiro
authors.initials: M
authors.lastname: Higuchi
authors.forename: Takatoshi
authors.initials: T
authors.lastname: Kinoshita
authors.forename: Nobuyuki
authors.initials: N
authors.lastname: Higashi
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D049329:Nanostructures / Q000737:chemistry*; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: C509030:LKL16 peptide; D009842:Oligopeptides