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Controlling Mineralization with Protein-Functionalized Peptoid Nanotubes.

Jinrong Ma1, Biao Jin2, Kathryn N Guye3

  • 1Molecular Engineering and Science Institute, University of Washington, Seattle, WA, 98115, USA.

Advanced Materials (Deerfield Beach, Fla.)
|October 25, 2022
PubMed
Summary

Sequence-defined foldamers functionalized with solid-binding proteins enable precise control over inorganic nanocrystal synthesis. This method allows tuning of crystal size and creation of hybrid photocatalysts.

Keywords:
biomimetic mineralizationhierarchical architectureshybrid materialsphotocatalysissequence-defined biomolecules

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Area of Science:

  • Materials Science
  • Nanotechnology
  • Biomaterials Engineering

Background:

  • Sequence-defined foldamers offer precise control for templating inorganic mineralization.
  • Achieving robust control over nucleation and growth remains a challenge without extensive redesign.

Purpose of the Study:

  • To develop a method for controlled synthesis of inorganic nanocrystals using functionalized foldamers.
  • To tune crystallite size and create hybrid materials for photocatalysis.

Main Methods:

  • Utilized peptoid nanotubes functionalized with solid-binding proteins.
  • Mineralized homogeneously distributed and monodisperse anatase nanocrystals from TiBALDH precursor.
  • Tuned crystallite size by altering protein coverage and engineered segments.

Main Results:

  • Achieved systematic tuning of crystallite size (1.4–4.4 nm) for anatase nanocrystals.
  • Successfully synthesized gold nanoparticles and titania/gold nanocomposites.
  • Demonstrated photocatalytic activity of the hybrid nanocomposites under visible light.

Conclusions:

  • Hierarchical organization and denticity of solid-binding proteins critically influence mineralization outcomes.
  • This strategy provides a versatile platform for fabricating hierarchical hybrid materials with diverse inorganic components.