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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Protein Engineering

Background:

  • Morpheeins are proteins that alter morphology and function in response to environmental stimuli.
  • Peroxiredoxins (Prx) exhibit dual peroxidase and chaperone functions, changing from toroidal to tubular structures with pH shifts.
  • Previous research focused on 1D and 2D structures from toroidal Prx conformers, leaving higher-ordered materials unexplored.

Purpose of the Study:

  • To exploit the morpheein behavior of Prx for creating higher-ordered anisotropic materials.
  • To develop a bottom-up approach for assembling 3D anisotropic bundles using sequential stimuli.

Main Methods:

  • Utilized pH-dependent conformational changes of Prx (morpheeins).
  • Employed electrostatic recognition between negatively charged protein rims and positively charged porphyrins as molecular glue.
  • Applied sequential and orthogonal stimuli to guide self-assembly into 3D anisotropic bundles.

Main Results:

  • Successfully generated columnar aggregates of Prx through morpheein behavior.
  • Achieved self-assembly of these aggregates into 3D anisotropic bundles via porphyrin-mediated electrostatic interactions.
  • Demonstrated precise alignment of monodimensional stacks leading to anisotropic material formation.

Conclusions:

  • Morpheein behavior of Prx can be leveraged to construct complex 3D anisotropic materials.
  • This study presents a novel method for bottom-up fabrication of advanced metamaterials.
  • The findings open avenues for exploring higher-ordered structures from responsive proteins.