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Engineered a novel pH-sensitive short major ampullate spidroin.

Chen Zhang1, Jiali Mi1, Haishan Qi1

  • 1Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China; Frontier Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (MOE), School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300350, China; Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin University, Tianjin 300072, China.

International Journal of Biological Macromolecules
|March 22, 2020
PubMed
Summary

This study engineered a novel spider silk protein (NT-MaSp1s-CT) with pH-dependent structures. The resulting artificial spider silk exhibits a broad pH range for formation and excellent biocompatibility.

Keywords:
BiocompatibilityMicelleRecombinant spider silk proteinSynthetic biologypH-sensitive

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Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Polymer Chemistry

Background:

  • Spider silk proteins (spidroins) self-assembly is significantly influenced by pH.
  • Developing artificial spider silk with controlled assembly properties is crucial for advanced material applications.

Purpose of the Study:

  • To engineer a novel spider silk protein (NT-MaSp1s-CT) with pH-dependent secondary structures.
  • To investigate the self-assembly mechanism and spinning behavior of NT-MaSp1s-CT across a wide pH range.
  • To evaluate the biocompatibility of the fabricated artificial spider silk fibers.

Main Methods:

  • Construction of a recombinant spider silk protein (NT-MaSp1s-CT) incorporating pH-sensitive domains.
  • Characterization of protein secondary structures at varying pH conditions.
  • Micelles theory applied to analyze assembly in concentrated spinning dope.
  • Fiber spinning and assessment of fiber uniformity and continuity.
  • Hemolysis and cytotoxicity assays to determine biocompatibility.

Main Results:

  • NT-MaSp1s-CT demonstrated pH-dependent conformational transitions as designed.
  • Continuous and uniform artificial spider silk fibers were successfully spun across an unprecedented pH range (2-11).
  • The NT-MaSp1s-CT fibers exhibited excellent biocompatibility, with low hemolysis and cytotoxicity.

Conclusions:

  • The engineered NT-MaSp1s-CT protein offers a simplified and broad pH window for artificial spider silk production.
  • The protein's pH-dependent assembly and biocompatibility present significant potential for biomedical and pharmaceutical applications.
  • This work broadens the processing possibilities for artificial spider silk, facilitating its industrial and clinical translation.