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Controlled Mineralization with Protein-Functionalized Peptoid Nanotubesmics of Proteins on Surfaces

October 25, 2022

Ma Adv Mater Graphic.png

Conceptual illustration (top) and outcomes (bottom) of the biomimetic mineralization process.

Scientific Achievement

Developed a modular approach to controlling biomimetic mineralization and fabricating functional nanocomposites on peptoid scaffolds derivatized with solid-binding proteins.

Significance and Impact

Results show that both repetitive display and conformational flexibility of inorganic-binding segments are important in regulating mineralization and creating hierarchical materials.

Research Details

  • Used thiol-maleimide chemistry to conjugate proteins engineered to present one or more materials-specific solid-binding peptides to self-assembled peptoid nanotubes.

  • Showed that protein occupancy and solid-binding peptide sequence and valency systematically regulate the size of mineralized anatase nanocrystals in the 1.4 to 4.4 nm range through modulation of particle capping efficiency.

  • Extended the concept of Au mineralization and to the successive mineralization of TiO₂ and Au to produce nanotubes that are photocatalytically active under visible light illumination.

Ma, J., B. Jin, K.N. Guye, Md.E. Chowdhury, N.Y. Naser, C.L. Chen, J.J. De Yoreo, and F. Baneyx. (2022). Controlled mineralization with protein-functionalized peptoid nanotubes. Adv. Mater. DOI: 10.1002/adma.202207543

Work was performed at the University of Washington and PNNL using the UW Molecular Analysis Facility and the PNNL Environmental and Molecular Sciences Laboratory.

Thrust 1: Emergence of Order: Research


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