Shape-specific nanofibers via self-assembly of three-branched peptide

A novel amphiphilic branched peptide (1), in which three β-sheet formable peptides (L4K8L4) were connected by Lys residue, was newly prepared as a building block for self-assembly. A detailed analysis of the conformation and self-assembling property of 1 in water at various pH conditions was performed by using circular dichroism, FTIR, atomic force and transmission electron microscopies. The experimental results revealed that the branched peptide showed a pH-dependent conformation forming a shape-specific β-sheet-based nanofiber with morphologically kinked structures under specific pH conditions. Exploring a novel peptide building unit that has the ability to self-assemble into designed and complicated nano-objects is valuable to facilitate a bottom-up nanotechnology.

A novel amphiphilic three-armed peptide, in which three β-sheet formable peptides (L4K8L4) were connected by Lys residue, showed the pH-dependent self-assembly into shape-specific nanofibers with morphologically kinked structures.Figure optionsDownload high-quality image (43 K)Download as PowerPoint slideHighlights
► A novel amphiphilic branched peptide containing three β-sheet formable peptides was newly prepared as a building block for self-assembly.
► Conformation of the branched peptide could be easily controlled by manipulating the solution pH.
► The branched peptide was found to form a shape-specific β-sheet-based nanofiber with morphologically kinked structure via self-assembly.