Abstract
Self-assembly of artificial peptides has been widely studied for constructing nanostructured materials, with numerous potential applications in the nanobiotechnology field. Herein, we report the synthesis and hierarchical self-assembly of collagen-mimetic peptides (CMPs) bearing various aromatic groups at the N-termini, including 2-naphthyl, 1-naphtyl, anthracenyl, and pyrenyl groups, into nanofibers. The CMPs (R-(GPO)n: n > 4) formed a triple helix structure in water at 4 °C, as confirmed via CD analyses, and their conformations were more stable with increasing hydrophobicity of the terminal aromatic group and peptide chain length. The resulting pre-organized triple helical CMPs showed diverse self-assembly into highly ordered nanofibers, reflecting their slight differences in hydrophobic/hydrophilic balance and configuration of aromatic templates. TEM analysis demonstrated that 2Np-CMPn (n = 6 and 7) and Py-CMP6 provided well-developed natural collagen-like nanofibers and An-CMPn (n = 5–7) self-assembled into rod-like micelle fibers. On the other hand, 2Np-CMP5 and 1Np-CMP6 were unable to form nanofibers under the same conditions. Furthermore, the Py-CMP6 nanofiber was found to encapsulate a guest hydrophobic molecule, Nile red, and exhibited unique emission behavior based on the specific nanostructure. In addition to the ability of CMPs to bind small molecules, their controlled self-assembly enables their versatile utilization in drug delivery and wavelength-conversion nanomaterials.
Highlights
Significant efforts have been dedicated to the design of protein and peptidebased nanomaterials using a bottom-up approach with potential utility in biomedical and nanotechnology fields, such as tissue engineering, drug delivery, catalysis, and light harvesting [1,2,3,4,5,6]
Our group demonstrated that photo-responsive azobenzeneterminated collagen-mimetic peptides (CMPs) (9–24 mers) self-assembled into nanofibers and a hydrogel, in which the hydrophobic/hydrophilic balance had a significant effect on the fate of self-assembly
All the CMPs employed in this study consist of repeated units of the Gly-Pro-Hyp triplet, (GPO)n, which is well-known to be the most stable sequence for the triple helix structure [22] and aromatic groups at the N-terminus
Summary
Significant efforts have been dedicated to the design of protein and peptidebased nanomaterials using a bottom-up approach with potential utility in biomedical and nanotechnology fields, such as tissue engineering, drug delivery, catalysis, and light harvesting [1,2,3,4,5,6]. We prepared short CMPs bearing various aromatic groups: 2-naphthyl (2Np), 1-naphthyl (1Np), 2-anthracenyl (An), and 1-pyrenyl (Py), which are capable of self-assembly into versatile nanofibers.
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