Nanoparticle-Mediated Assembly of Peptoid Nanosheets Functionalized with Solid-Binding Proteins: Designing Heterostructures for Hierarchy
Abstract
The fabrication of ordered architectures that intimately integrate polymer, protein and inorganic components remains difficult. Two promising building blocks to tackle this challenge are peptoids, peptide mimics capable of self-assembly into well-defined structures, and solid-binding peptides, which offer a biological path to controlled inorganic assembly. Here, we report on the synthesis of 3.3 nm-thick, thiol-reactive peptoid nanosheets from equimolar mixtures of unmodified and maleimide-derivatized versions of the Nbpe6Nce6 oligomer, optimize the location of engineered cysteine residues in silica-binding derivatives of superfolder green fluorescent protein for maleimide conjugation, and react the two components to form proteinpeptoid hybrids exhibiting partial or uniform protein coverage on both of their sides. Using 10 nm silica nanoparticles, we trigger the stacking of these 2D structures into a multi-layer material comprised of alternating peptoid, protein and organic layers. This simple and modular approach to hierarchical hybrid synthesis should prove useful in bioimaging and photocatalysis applications.
- Authors:
-
[2];
[2];
[2];
[1]
- Univ. of Washington, Seattle, WA (United States). Molecular Engineering and Sciences Institute
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Publication Date:
- Research Org.:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States); Univ. of Washington, Seattle, WA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1778838
- Alternate Identifier(s):
- OSTI ID: 1781122
- Report Number(s):
- PNNL-SA-159754
Journal ID: ISSN 1530-6984
- Grant/Contract Number:
- AC05-76RL01830; SC0019288
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nano Letters
- Additional Journal Information:
- Journal Volume: 21; Journal Issue: 4; Journal ID: ISSN 1530-6984
- Publisher:
- American Chemical Society
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 77 NANOSCIENCE AND NANOTECHNOLOGY; peptoid; solid binding peptide; protein design; self-assembly
Citation Formats
Ma, Jinrong, Cai, Bin, Zhang, Shuai, Jian, Tengyue, De Yoreo, James J., Chen, Chun-Long, and Baneyx, François. Nanoparticle-Mediated Assembly of Peptoid Nanosheets Functionalized with Solid-Binding Proteins: Designing Heterostructures for Hierarchy. United States: N. p., 2021.
Web. doi:10.1021/acs.nanolett.0c04285.
Ma, Jinrong, Cai, Bin, Zhang, Shuai, Jian, Tengyue, De Yoreo, James J., Chen, Chun-Long, & Baneyx, François. Nanoparticle-Mediated Assembly of Peptoid Nanosheets Functionalized with Solid-Binding Proteins: Designing Heterostructures for Hierarchy. United States. https://doi.org/10.1021/acs.nanolett.0c04285
Ma, Jinrong, Cai, Bin, Zhang, Shuai, Jian, Tengyue, De Yoreo, James J., Chen, Chun-Long, and Baneyx, François. Mon .
"Nanoparticle-Mediated Assembly of Peptoid Nanosheets Functionalized with Solid-Binding Proteins: Designing Heterostructures for Hierarchy". United States. https://doi.org/10.1021/acs.nanolett.0c04285. https://www.osti.gov/servlets/purl/1778838.
@article{osti_1778838,
title = {Nanoparticle-Mediated Assembly of Peptoid Nanosheets Functionalized with Solid-Binding Proteins: Designing Heterostructures for Hierarchy},
author = {Ma, Jinrong and Cai, Bin and Zhang, Shuai and Jian, Tengyue and De Yoreo, James J. and Chen, Chun-Long and Baneyx, François},
abstractNote = {The fabrication of ordered architectures that intimately integrate polymer, protein and inorganic components remains difficult. Two promising building blocks to tackle this challenge are peptoids, peptide mimics capable of self-assembly into well-defined structures, and solid-binding peptides, which offer a biological path to controlled inorganic assembly. Here, we report on the synthesis of 3.3 nm-thick, thiol-reactive peptoid nanosheets from equimolar mixtures of unmodified and maleimide-derivatized versions of the Nbpe6Nce6 oligomer, optimize the location of engineered cysteine residues in silica-binding derivatives of superfolder green fluorescent protein for maleimide conjugation, and react the two components to form proteinpeptoid hybrids exhibiting partial or uniform protein coverage on both of their sides. Using 10 nm silica nanoparticles, we trigger the stacking of these 2D structures into a multi-layer material comprised of alternating peptoid, protein and organic layers. This simple and modular approach to hierarchical hybrid synthesis should prove useful in bioimaging and photocatalysis applications.},
doi = {10.1021/acs.nanolett.0c04285},
journal = {Nano Letters},
number = 4,
volume = 21,
place = {United States},
year = {Mon Feb 08 00:00:00 EST 2021},
month = {Mon Feb 08 00:00:00 EST 2021}
}
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