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Cell-Free Nonequilibrium Assembly for Hierarchical Protein/Peptide Nanopillars.

Jiaqi Guo1, Ayisha Zia2, Qianfeng Qiu1

  • 1Department of Chemistry, Brandeis University, 415 South St., Waltham, Massachusetts 02453, United States.

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|September 10, 2024
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Researchers created cell-free protein nanopillars using enzyme-responsive peptides and nonequilibrium self-assembly. This method mimics natural structures and allows for controlled recruitment of other proteins like collagen.

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Cellular Biology

Background:

  • Cells possess complex protein nanostructures that are difficult to replicate outside of cellular environments.
  • Vertical fibronectin pillars in embryos serve as a model for intricate, naturally occurring protein assemblies.
  • Existing methods face challenges in recreating the directional growth and composition of these cellular structures.

Purpose of the Study:

  • To develop a cell-free method for creating vertical fibronectin pillar mimics.
  • To investigate the use of enzyme-responsive phosphopeptides in nonequilibrium self-assembly for nanostructure formation.
  • To control the recruitment and organization of other proteins, such as collagen, within the assembled structures.

Main Methods:

  • Utilized enzyme-responsive phosphopeptides that self-assemble into nanotubes.
  • Employed enzyme action to induce shape changes and drive vertical growth of protein nanopillars.
  • Leveraged peptide nanotubes as templates to remodel fibronectin and recruit collagen.
  • Analyzed structures using Cryo-electron microscopy (Cryo-EM).

Main Results:

  • Successfully created cell-free vertical fibronectin pillar mimics via nonequilibrium self-assembly.
  • Demonstrated enzyme-catalyzed growth of protein nanopillars into bundles, templated by nanotubes.
  • Showcased recruitment of collagen, forming aggregates or bundles based on collagen type.
  • Observed nanotube thinning and packing post-dephosphorylation via Cryo-EM, indicating complex assembly dynamics.

Conclusions:

  • Established a novel cell-free approach for constructing directed, multiprotein nanostructures.
  • Highlighted the role of enzyme-catalyzed nonequilibrium self-assembly in building complex nanoscale architectures.
  • Provided insights into the dynamic sculpting processes during peptide and protein assembly.