| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 608632 | Journal of Colloid and Interface Science | 2011 | 5 Pages |
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.
Graphical abstractA 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 full-size imageDownload 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.
