A Rationally Designed Supercharged Protein-Enzyme Chimera Self-Assembles In Situ to Yield Bifunctional Composite Textiles.

Graham J Day; William H Zhang; Ben Carter; Wenjin Xiao; Mark R. Sambrook; Adam W Perriman

doi:10.1021/acsami.1c18857

A Rationally Designed Supercharged Protein-Enzyme Chimera Self-Assembles In Situ to Yield Bifunctional Composite Textiles.

Graham J Day, William H Zhang, Ben Carter, Wenjin Xiao, Mark R. Sambrook, Adam W Perriman^*

^*Corresponding author for this work

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Abstract

Catalytically active materials for the enhancement of personalized protective equipment (PPE) could be advantageous to help alleviate threats posed by neurotoxic organophosphorus compounds (OPs). Accordingly, a chimeric protein comprised of a supercharged green fluorescent protein (scGFP) and phosphotriesterase from Agrobacterium radiobacter (arPTE) was designed to drive the polymer surfactant (S–)-mediated self-assembly of microclusters to produce robust, enzymatically active materials. The chimera scGFP-arPTE was structurally characterized via circular dichroism spectroscopy and synchrotron radiation small-angle X-ray scattering, and its biophysical properties were determined. Significantly, the chimera exhibited greater thermal stability than the native constituent proteins, as well as a higher catalytic turnover number (kcat). Furthermore, scGFP-arPTE was electrostatically complexed with monomeric S–, driving self-assembly into [scGFP-arPTE][S–] nanoclusters, which could be dehydrated and cross-linked to yield enzymatically active [scGFP-arPTE][S–] porous films with a high-order structure. Moreover, these clusters could self-assemble within cotton fibers to generate active composite textiles without the need for the pretreatment of the fabrics. Significantly, the resulting materials maintained the biophysical activities of both constituent proteins and displayed recyclable and persistent activity against the nerve agent simulant paraoxon.

Original language	English
Pages (from-to)	60433−60445
Number of pages	13
Journal	ACS Applied Materials and Interfaces
Volume	13
Issue number	50
Early online date	13 Dec 2021
DOIs	https://doi.org/10.1021/acsami.1c18857
Publication status	Published - 22 Dec 2021

Bibliographical note

Funding Information:
This research was funded by the Defence Science and Technology Laboratory (Dstl) and we thank them for this. We thank EPSRC (Early Career Fellowship EP/K026720/1) and UKRI (Future Leaders Fellowship MR/ S016430/1) for the support of Professor Adam W. Perriman. We are grateful for the time allocation from Diamond Light Source, which allowed SR–S/WAXS experiments to be performed on the I22 beamline (proposal SM17972) and bio-SAXS on the B21 beamline (proposal SM16970). We would like to thank the beamline scientists for their help. We would also like to acknowledge the Wolfson Bioimaging Centre (BBSRC Alert 13 capital grant BB/L014181/1) at the University of Bristol.

Publisher Copyright:
© 2021 American Chemical Society

Keywords

composite material
active material
hierarchical self-assembly
bifunctionality
catalysis
decontamination
enzyme

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Accepted author manuscript, 1.66 MB

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title = "A Rationally Designed Supercharged Protein-Enzyme Chimera Self-Assembles In Situ to Yield Bifunctional Composite Textiles.",

abstract = "Catalytically active materials for the enhancement of personalized protective equipment (PPE) could be advantageous to help alleviate threats posed by neurotoxic organophosphorus compounds (OPs). Accordingly, a chimeric protein comprised of a supercharged green fluorescent protein (scGFP) and phosphotriesterase from Agrobacterium radiobacter (arPTE) was designed to drive the polymer surfactant (S–)-mediated self-assembly of microclusters to produce robust, enzymatically active materials. The chimera scGFP-arPTE was structurally characterized via circular dichroism spectroscopy and synchrotron radiation small-angle X-ray scattering, and its biophysical properties were determined. Significantly, the chimera exhibited greater thermal stability than the native constituent proteins, as well as a higher catalytic turnover number (kcat). Furthermore, scGFP-arPTE was electrostatically complexed with monomeric S–, driving self-assembly into [scGFP-arPTE][S–] nanoclusters, which could be dehydrated and cross-linked to yield enzymatically active [scGFP-arPTE][S–] porous films with a high-order structure. Moreover, these clusters could self-assemble within cotton fibers to generate active composite textiles without the need for the pretreatment of the fabrics. Significantly, the resulting materials maintained the biophysical activities of both constituent proteins and displayed recyclable and persistent activity against the nerve agent simulant paraoxon.",

keywords = "composite material, active material, hierarchical self-assembly, bifunctionality, catalysis, decontamination, enzyme",

author = "Day, {Graham J} and Zhang, {William H} and Ben Carter and Wenjin Xiao and Sambrook, {Mark R.} and Perriman, {Adam W}",

note = "Funding Information: This research was funded by the Defence Science and Technology Laboratory (Dstl) and we thank them for this. We thank EPSRC (Early Career Fellowship EP/K026720/1) and UKRI (Future Leaders Fellowship MR/ S016430/1) for the support of Professor Adam W. Perriman. We are grateful for the time allocation from Diamond Light Source, which allowed SR–S/WAXS experiments to be performed on the I22 beamline (proposal SM17972) and bio-SAXS on the B21 beamline (proposal SM16970). We would like to thank the beamline scientists for their help. We would also like to acknowledge the Wolfson Bioimaging Centre (BBSRC Alert 13 capital grant BB/L014181/1) at the University of Bristol. Publisher Copyright: {\textcopyright} 2021 American Chemical Society",

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AU - Day, Graham J

AU - Zhang, William H

AU - Carter, Ben

AU - Xiao, Wenjin

AU - Sambrook, Mark R.

AU - Perriman, Adam W

N1 - Funding Information: This research was funded by the Defence Science and Technology Laboratory (Dstl) and we thank them for this. We thank EPSRC (Early Career Fellowship EP/K026720/1) and UKRI (Future Leaders Fellowship MR/ S016430/1) for the support of Professor Adam W. Perriman. We are grateful for the time allocation from Diamond Light Source, which allowed SR–S/WAXS experiments to be performed on the I22 beamline (proposal SM17972) and bio-SAXS on the B21 beamline (proposal SM16970). We would like to thank the beamline scientists for their help. We would also like to acknowledge the Wolfson Bioimaging Centre (BBSRC Alert 13 capital grant BB/L014181/1) at the University of Bristol. Publisher Copyright: © 2021 American Chemical Society

PY - 2021/12/22

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N2 - Catalytically active materials for the enhancement of personalized protective equipment (PPE) could be advantageous to help alleviate threats posed by neurotoxic organophosphorus compounds (OPs). Accordingly, a chimeric protein comprised of a supercharged green fluorescent protein (scGFP) and phosphotriesterase from Agrobacterium radiobacter (arPTE) was designed to drive the polymer surfactant (S–)-mediated self-assembly of microclusters to produce robust, enzymatically active materials. The chimera scGFP-arPTE was structurally characterized via circular dichroism spectroscopy and synchrotron radiation small-angle X-ray scattering, and its biophysical properties were determined. Significantly, the chimera exhibited greater thermal stability than the native constituent proteins, as well as a higher catalytic turnover number (kcat). Furthermore, scGFP-arPTE was electrostatically complexed with monomeric S–, driving self-assembly into [scGFP-arPTE][S–] nanoclusters, which could be dehydrated and cross-linked to yield enzymatically active [scGFP-arPTE][S–] porous films with a high-order structure. Moreover, these clusters could self-assemble within cotton fibers to generate active composite textiles without the need for the pretreatment of the fabrics. Significantly, the resulting materials maintained the biophysical activities of both constituent proteins and displayed recyclable and persistent activity against the nerve agent simulant paraoxon.

AB - Catalytically active materials for the enhancement of personalized protective equipment (PPE) could be advantageous to help alleviate threats posed by neurotoxic organophosphorus compounds (OPs). Accordingly, a chimeric protein comprised of a supercharged green fluorescent protein (scGFP) and phosphotriesterase from Agrobacterium radiobacter (arPTE) was designed to drive the polymer surfactant (S–)-mediated self-assembly of microclusters to produce robust, enzymatically active materials. The chimera scGFP-arPTE was structurally characterized via circular dichroism spectroscopy and synchrotron radiation small-angle X-ray scattering, and its biophysical properties were determined. Significantly, the chimera exhibited greater thermal stability than the native constituent proteins, as well as a higher catalytic turnover number (kcat). Furthermore, scGFP-arPTE was electrostatically complexed with monomeric S–, driving self-assembly into [scGFP-arPTE][S–] nanoclusters, which could be dehydrated and cross-linked to yield enzymatically active [scGFP-arPTE][S–] porous films with a high-order structure. Moreover, these clusters could self-assemble within cotton fibers to generate active composite textiles without the need for the pretreatment of the fabrics. Significantly, the resulting materials maintained the biophysical activities of both constituent proteins and displayed recyclable and persistent activity against the nerve agent simulant paraoxon.

KW - composite material

KW - active material

KW - hierarchical self-assembly

KW - bifunctionality

KW - catalysis

KW - decontamination

KW - enzyme

U2 - 10.1021/acsami.1c18857

DO - 10.1021/acsami.1c18857

M3 - Article (Academic Journal)

C2 - 34894651

VL - 13

SP - 60433−60445

JO - ACS Applied Materials and Interfaces

JF - ACS Applied Materials and Interfaces

SN - 1944-8244

IS - 50

ER -

A Rationally Designed Supercharged Protein-Enzyme Chimera Self-Assembles In Situ to Yield Bifunctional Composite Textiles.

Abstract

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Keywords

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