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Title: Templated Assembly of a Functional Ordered Protein Macromolecular Framework from P22 Virus-like Particles

Abstract

Bottom-up construction of mesoscale materials using biologically derived nanoscale building blocks enables engineering of desired physical properties using green production methods. Virus-like particles (VLPs) are exceptional building blocks due to their monodispersed sizes, geometric shapes, production ease, proteinaceous composition, and our ability to independently functionalize the interior and exterior interfaces. Here a VLP, derived from bacteriophage P22, is used as a building block for the fabrication of a protein macromolecular framework (PMF), a tightly linked 3D network of functional protein cages that exhibit long-range order and catalytic activity. Assembly of PMFs was electrostatically templated, using amine-terminated dendrimers, then locked into place with a ditopic cementing protein that binds to P22. Long-range order is preserved on removal of the dendrimer, leaving a framework material composed completely of protein. Furthermore, encapsulation of β-glucosidase enzymes inside of P22 VLPs results in formation of stable, condensed-phase materials with high local concentration of enzymes generating catalytically active PMFs.

Authors:
 [1]; ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [1]
  1. Indiana Univ., Bloomington, IN (United States)
  2. Argonne National Lab. (ANL), Argonne, IL (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1461340
Grant/Contract Number:  
AC02-06CH11357
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
ACS Nano
Additional Journal Information:
Journal Volume: 12; Journal Issue: 4; Journal ID: ISSN 1936-0851
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English
Subject:
77 NANOSCIENCE AND NANOTECHNOLOGY; catalytic material; decoration protein; nanoreactor; protein framework; self-assembly; templated assembly; virus-like particle (VLP)

Citation Formats

McCoy, Kimberly, Uchida, Masaki, Lee, Byeongdu, and Douglas, Trevor. Templated Assembly of a Functional Ordered Protein Macromolecular Framework from P22 Virus-like Particles. United States: N. p., 2018. Web. doi:10.1021/acsnano.8b00528.
McCoy, Kimberly, Uchida, Masaki, Lee, Byeongdu, & Douglas, Trevor. Templated Assembly of a Functional Ordered Protein Macromolecular Framework from P22 Virus-like Particles. United States. doi:10.1021/acsnano.8b00528.
McCoy, Kimberly, Uchida, Masaki, Lee, Byeongdu, and Douglas, Trevor. Tue . "Templated Assembly of a Functional Ordered Protein Macromolecular Framework from P22 Virus-like Particles". United States. doi:10.1021/acsnano.8b00528. https://www.osti.gov/servlets/purl/1461340.
@article{osti_1461340,
title = {Templated Assembly of a Functional Ordered Protein Macromolecular Framework from P22 Virus-like Particles},
author = {McCoy, Kimberly and Uchida, Masaki and Lee, Byeongdu and Douglas, Trevor},
abstractNote = {Bottom-up construction of mesoscale materials using biologically derived nanoscale building blocks enables engineering of desired physical properties using green production methods. Virus-like particles (VLPs) are exceptional building blocks due to their monodispersed sizes, geometric shapes, production ease, proteinaceous composition, and our ability to independently functionalize the interior and exterior interfaces. Here a VLP, derived from bacteriophage P22, is used as a building block for the fabrication of a protein macromolecular framework (PMF), a tightly linked 3D network of functional protein cages that exhibit long-range order and catalytic activity. Assembly of PMFs was electrostatically templated, using amine-terminated dendrimers, then locked into place with a ditopic cementing protein that binds to P22. Long-range order is preserved on removal of the dendrimer, leaving a framework material composed completely of protein. Furthermore, encapsulation of β-glucosidase enzymes inside of P22 VLPs results in formation of stable, condensed-phase materials with high local concentration of enzymes generating catalytically active PMFs.},
doi = {10.1021/acsnano.8b00528},
journal = {ACS Nano},
issn = {1936-0851},
number = 4,
volume = 12,
place = {United States},
year = {2018},
month = {3}
}

Journal Article:
Free Publicly Available Full Text
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Cited by: 2 works
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