Recombinant self-assembling 16-residue peptide nanofiber scaffolds for neuronal axonal outgrowth

Peng Liang, Jinsheng Xiong, Liwei Zhao, Ye Xu, Jiaxin Zhao, Qing Liu

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Self-assembling peptides are considered a good biological scaffold for the repair of injured nervous system. In order to set up a stable system to produce the peptides at low cost, we used a gene recombinant expression method. The sequence of the peptide was devised to facilitate neural cell attachment and growth. The nucleotide sequence of the self-assembling peptide was designed, artificially synthesized, and inserted into the fusion protein vector pTYB2. After being transformed and expressed in Escherichia coli BL-21 (DE3) by means of the fusion protein, the soluble 16-residue peptide (named RAE16) was obtained by one-step chitin affinity chromatography. During cell culture, bone marrow stromal cells were fully embedded in the 3D environment of the peptide scaffolds. The MTT (3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2-H-tetrazolium bromide) test indicated that bone marrow stromal cells cultured in RAE16 had the highest survival rate with the absorbance value of 0.7 at 7 days. Moreover, the cortical neural axons in the RAE16 group were longer (118.36 ± 7.04 μm) than in the other groups (p < 0.01). The recombinant peptide nanofiber scaffolds we designed provide a promising cell culture system for general molecular and cell biology studies and are useful as well for neural regeneration studies.

Original languageEnglish (US)
Pages (from-to)152-158
Number of pages7
JournalEngineering in Life Sciences
Issue number1
StatePublished - Jan 1 2015
Externally publishedYes


  • Axonal outgrowth
  • Neuron
  • Protein expression
  • Self-assembled nanofiber scaffold
  • Tissue engineering

ASJC Scopus subject areas

  • Biotechnology
  • Environmental Engineering
  • Bioengineering


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