Layered Heterostructures from Nanoparticle-Mediated Assembly of Protein-Modified Peptoid Nanosheets

February 8, 2021

Crystalline peptoid nanosheets prepared at equimolar concentrations of Nbpe₆Nce₆ and MAL-Nbpe₆Nce₆ monomers are reacted with silica-binding derivatives of superfolder green fluorescent protein engineered with the G51C/C48S substitutions. 10-nm silica nanoparticles drive the self-assembly of a multilayer material with alternating compositions. 

Scientific Achievement

2D peptoid nanosheets functionalized with silica-binding proteins self-assemble into a material with alternating peptoid, protein and inorganic layers upon addition of silica nanoparticles.

Significance and Impact

This work demonstrates a path for facile and modular fabrication of multi-component hierarchical materials.

Research Details

  • The placement of cysteine residues on solid-binding proteins is optimized to maximize reactivity with peptoid nanosheets prepared with an equimolar amount of maleimide-modified peptoid oligomers.

  • Addition of silica nanoparticles triggers stacking of these 2D nanostructures into a 3D multilayer material.

  • Inorganic adhesion zones can be patchy or continuous depending on protein concentration.

Ma, J., B. Cai, S. Zhang, T. Jian, J.J. De Yoreo, C-L Chen, and F. Baneyx. (2021). Nanoparticle-mediated assembly of peptoid nanosheets functionalized with solid-binding proteins: Designing heterostructures for hierarchy. Nano Letters 21: 1636-1642. DOI: 10.1021/acs.nanolett.0c04285

Work performed at the University of Washington and Pacific Northwest National Laboratory



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