A novel amphiphilic branched peptide (1), in which three β-sheet formable peptides (L(4)K(8)L(4)) 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.
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