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

• Published in: Journal of colloid and interface science Vol. 358; no. 1; pp. 81 - 85
• Main Authors: Koga, Tomoyuki, Matsui, Harunobu, Matsumoto, Takahiro, Higashi, Nobuyuki
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 01.06.2011; Elsevier
• Subjects: Amino Acid Sequence; Branched; Chemistry; Exact sciences and technology; Fourier transform infrared spectroscopy; General and physical chemistry; Hydrogen-Ion Concentration; Leucine - chemistry; Lysine - chemistry; Molecular Sequence Data; Nanofiber; Nanofibers; Nanofibers - chemistry; Nanofibers - ultrastructure; Nanomaterials; Nanostructure; Nanotechnology; Peptides; Peptides - chemistry; Protein Structure, Secondary; Self assembly; Shape-specificity; Surface-Active Agents - chemistry; Three-branched peptide; transmission electron microscopy; β-Sheet structure; Shape-specificity; Nanofiber; Self-assembly; Three-branched peptide; β-Sheet structure; Water; Self assembly; Shape; Peptides; Force; Circular dichroism; Design; Infrared spectrometry; Transmission electron microscopy; Residue; pH; Structure; Nanotechnology; Conformation
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1016/j.jcis.2011.02.055

A novel amphiphilic three-armed peptide, in which three β-sheet formable peptides (L 4K 8L 4) were connected by Lys residue, showed the pH-dependent self-assembly into shape-specific nanofibers with morphologically kinked structures. [Display omitted] ► 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. A novel amphiphilic branched peptide ( 1), in which three β-sheet formable peptides (L 4K 8L 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.