Tubular Network Formation by Mixing Amphiphilic Polypeptides with Differing Hydrophilic Blocks

Md Mofizur Rahman, Motoki Ueda*, Kon Son, Siyoong Seo, Shinji Takeoka, Takuji Hirose, Yoshihiro Ito

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Artificial tubular networks are promising structures for biomaterial applications because of their large surface areas. A tubular network was formed by co-assembling two different amphiphilic polypeptides, poly(ethylene glycol)-b-(l-Leu-Aib)6 (PL12) and polysarcosine-b-(l-Leu-Aib)6 (SL12). They both have the same hydrophobic 12-mer helical block (l-Leu-Aib)6 but different hydrophilic chains, poly(ethylene glycol) and polysarcosine. In water, both polypeptides self-assembled into a tubular structure having a uniform 80 nm diameter that was formed by packing among the hydrophobic L12 blocks. The SL12 nanotubes were short (200 nm), straight, and robust. PL12 formed long (>1 μm), bendable, and fusogenic nanotubes. The amphiphiles were then co-assembled with various mixing ratios to form tubular networks. Higher concentrations of PL12 made the nanotubes more bendable and fusogenic between open tube ends, which produced branching junctions under heat treatment.

Original languageEnglish
Pages (from-to)3908-3914
Number of pages7
Issue number10
Publication statusPublished - 2019 Oct 14

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry


Dive into the research topics of 'Tubular Network Formation by Mixing Amphiphilic Polypeptides with Differing Hydrophilic Blocks'. Together they form a unique fingerprint.

Cite this