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Synthesis of an Intein-mediated Artificial Protein Hydrogel
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Programmed Protein Self-Assembly Driven by Genetically Encoded Intein-Mediated Native Chemical Ligation.

Joseph A Harvey1, Laura S Itzhaki2, Ewan R G Main1

  • 1School of Biological and Chemical Sciences Queen Mary, University of London , Mile End Road , London E1 4NS , United Kingdom.

ACS Synthetic Biology
|February 24, 2018
PubMed
Summary

Researchers developed a system for precise protein assembly using iterative intein-mediated native chemical ligation (NCL). This method allows controlled construction of novel protein-based biomaterials with specific arrangements and functions.

Keywords:
directed protein assemblyexpressed intein ligationnanostructuresnative chemical ligationprotein designtraceless protein conjugation

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Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Synthetic Biology

Background:

  • Controlling protein self-assembly is crucial for developing advanced protein-based biomaterials.
  • Existing methods often lack precision in directing the arrangement and concatenation of multiple protein domains.

Purpose of the Study:

  • To design a general, genetically programmed system for the controlled, covalent assembly of distinct protein domains into specific arrays.
  • To enable the precise construction of novel protein-based biomaterials with user-defined architectures.

Main Methods:

  • Utilized iterative intein-mediated native chemical ligation (NCL) under mild, native conditions.
  • Employed a system of recombinant protein fusions with orthogonal activation via protease and intein cleavage.
  • Implemented sequential mixing strategies for stepwise, irreversible, and traceless protein assembly.

Main Results:

  • Demonstrated a system for covalently concatenating multiple protein domains into specific, ordered arrays.
  • Achieved precise control over the composition and arrangement of proteins in the final assembled product.
  • Successfully produced "functional" protein assemblies, validating the system's capabilities.

Conclusions:

  • The developed system offers a powerful tool for engineering complex protein architectures.
  • This approach facilitates the creation of novel protein biomaterials with tailored properties and functions.
  • The method provides a general platform for investigating the efficiency and yield limits of protein assembly processes.