Self-assembling bolaamphiphile-like collagen mimetic peptides

Abstract

The extraordinary biological and structural features of collagen has aroused great interest to construct collagen mimetic materials with promising applications in tissue engineering and regenerative medicine. We herein report the construction of a novel family of bolaamphiphile-like collagen mimetic peptides composed of only natural amino acids. The peptides possess two hydrophilic heads consisting of charged aspartic acids, which are connected by the repetitive triple helical sequences typical of collagen. We have demonstrated that the terminal aspartic acids play an essential role in the self-assembly of bolaamphiphile-like collagen mimetic peptides, and their presence is required to trigger the self-assembly. We have shown that bolaamphiphile-like collagen mimetic peptides containing either (GPO)_m or (PPG)_m triplets consistently result in well-ordered nanospheres, suggesting that the amino acid content of collagen peptides may not affect their appropriate self-assembly. Both peptides D₂(GPO)₇D₂ and D₂(PPG)₁₂D₂ steadily lead to exquisite nanospheres under a broad range of pH conditions, indicating that these bolaamphiphile-like collagen mimetic peptides with charged aspartic acids at both terminals may provide a facile peptide-based approach to construct well-defined nanostructures. Bolaamphiphile-like peptides would greatly expand current strategies for self-assembling collagen peptides, aiding the discovery of improved functional biomaterials.