Structural control of self-assembled nanofibers by artificial beta-sheet peptides composed of D- or L-isomer.
A novel method for the control of peptide self-assembly has been developed by using synthetic triblock-type beta-sheet peptides composed of l- or d-amino acid, 1L and 1D, as building blocks. The peptides 1L and 1D self-assemble into beta-sheet nanofibers with left- and right-handed twists, respectively, under appropriate condition. On the other hand, the 1L/1D binary mixture was found to form only globular aggregates at the same condition. Thus, amyloid-like nanofiber formation and its nanostructure could be successfully regulated by the stereospecificity of the constituent peptide species.
Koga
Tomoyuki
T
Department of Molecular Science and Technology, Faculty of Engineering, Doshisha University, Kyotanabe, Kyoto 610-0321, Japan.
Matsuoka
Miho
M
Higashi
Nobuyuki
N
D000682:Amyloid / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry; D002942:Circular Dichroism; D031541:Fluorescence Resonance Energy Transfer; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D007930:Leucine / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013237:Stereoisomerism; D001613:beta 2-Microglobulin / Q000737:chemistry
D000682:Amyloid; D016229:Amyloid beta-Peptides; D009842:Oligopeptides; D001613:beta 2-Microglobulin; D007930:Leucine; D008239:Lysine