Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size

Ioatzin Ríos de Anda; Angélique Coutable-Pennarun; Christopher Brasnett; Stephen Whitelam; Annela Seddon; John Russo; J L Ross Anderson; C Patrick Royall

doi:10.1039/d0sm02269a

Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size

Ioatzin Ríos de Anda, Angélique Coutable-Pennarun, Christopher Brasnett, Stephen Whitelam, Annela Seddon, John Russo, J L Ross Anderson, C Patrick Royall

Research output: Contribution to journal › Article (Academic Journal) › peer-review

3 Citations (Scopus)

52 Downloads (Pure)

Abstract

Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy - or electron - transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks.

Original language	English
Pages (from-to)	6873-6883
Number of pages	11
Journal	Soft Matter
Volume	17
Issue number	28
Early online date	30 Jun 2021
DOIs	https://doi.org/10.1039/d0sm02269a
Publication status	Published - 28 Jul 2021

Bibliographical note

Funding Information:
The authors would like to thank Nicholas Wood, Yushi Yang and Levke Ortlieb for providing the code for image analysis. The authors are grateful for very enriching discussions with Peter Schurtenberger and Bob Evans, and to Jennifer McManus for a critical reading of the manuscript. The work of IRdA and JR was funded by a Leverhulme Trust Philip Leverhulme Prize. IRdA was supported by a doctoral scholarship from CONACyT. JR acknowledges support from the European Research Council Grant DLV-75918. IRdA, AC-P and CPR gratefully acknowledge the ERC Grant agreement no. 617266 ‘‘NANOPRS’’ for financial support and Engineering and Physical Sciences Research Council (EP/H022333/1). The Ganesha X-ray scattering apparatus used for this research was purchased under EPSRC Grant ‘‘Atoms to Applications’’ (EP/K035746/1). This work benefitted from the SasView software, originally developed by the DANSE project under NSF award DMR-0520547.

Publisher Copyright:
© The Royal Society of Chemistry 2021.

Research Groups and Themes

BrisSynBio
Bristol BioDesign Institute

Keywords

Synthetic biology

Access to Document

10.1039/d0sm02269a

Full-text PDF (final published version)
This is the final published version of the article (version of record). It first appeared online via Royal Society of Chemistry at https://pubs.rsc.org/en/content/articlelanding/2021/sm/d0sm02269a#!divAbstract . Please refer to any applicable terms of use of the publisher.
Final published version, 4.16 MBLicence: CC BY-NC

Handle.net

Persistent link

Cite this

@article{d80bb533846c4e449ed782681870edac,

title = "Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size",

abstract = "Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy - or electron - transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks.",

keywords = "Synthetic biology",

author = "{R{\'i}os de Anda}, Ioatzin and Ang{\'e}lique Coutable-Pennarun and Christopher Brasnett and Stephen Whitelam and Annela Seddon and John Russo and Anderson, {J L Ross} and Royall, {C Patrick}",

note = "Funding Information: The authors would like to thank Nicholas Wood, Yushi Yang and Levke Ortlieb for providing the code for image analysis. The authors are grateful for very enriching discussions with Peter Schurtenberger and Bob Evans, and to Jennifer McManus for a critical reading of the manuscript. The work of IRdA and JR was funded by a Leverhulme Trust Philip Leverhulme Prize. IRdA was supported by a doctoral scholarship from CONACyT. JR acknowledges support from the European Research Council Grant DLV-75918. IRdA, AC-P and CPR gratefully acknowledge the ERC Grant agreement no. 617266 {\textquoteleft}{\textquoteleft}NANOPRS{\textquoteright}{\textquoteright} for financial support and Engineering and Physical Sciences Research Council (EP/H022333/1). The Ganesha X-ray scattering apparatus used for this research was purchased under EPSRC Grant {\textquoteleft}{\textquoteleft}Atoms to Applications{\textquoteright}{\textquoteright} (EP/K035746/1). This work benefitted from the SasView software, originally developed by the DANSE project under NSF award DMR-0520547. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2021.",

year = "2021",

month = jul,

day = "28",

doi = "10.1039/d0sm02269a",

language = "English",

volume = "17",

pages = "6873--6883",

journal = "Soft Matter",

issn = "1744-683X",

publisher = "Royal Society of Chemistry",

number = "28",

}

TY - JOUR

T1 - Decorated networks of native proteins

T2 - nanomaterials with tunable mesoscopic domain size

AU - Ríos de Anda, Ioatzin

AU - Coutable-Pennarun, Angélique

AU - Brasnett, Christopher

AU - Whitelam, Stephen

AU - Seddon, Annela

AU - Russo, John

AU - Anderson, J L Ross

AU - Royall, C Patrick

N1 - Funding Information: The authors would like to thank Nicholas Wood, Yushi Yang and Levke Ortlieb for providing the code for image analysis. The authors are grateful for very enriching discussions with Peter Schurtenberger and Bob Evans, and to Jennifer McManus for a critical reading of the manuscript. The work of IRdA and JR was funded by a Leverhulme Trust Philip Leverhulme Prize. IRdA was supported by a doctoral scholarship from CONACyT. JR acknowledges support from the European Research Council Grant DLV-75918. IRdA, AC-P and CPR gratefully acknowledge the ERC Grant agreement no. 617266 ‘‘NANOPRS’’ for financial support and Engineering and Physical Sciences Research Council (EP/H022333/1). The Ganesha X-ray scattering apparatus used for this research was purchased under EPSRC Grant ‘‘Atoms to Applications’’ (EP/K035746/1). This work benefitted from the SasView software, originally developed by the DANSE project under NSF award DMR-0520547. Publisher Copyright: © The Royal Society of Chemistry 2021.

PY - 2021/7/28

Y1 - 2021/7/28

N2 - Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy - or electron - transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks.

AB - Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy - or electron - transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks.

KW - Synthetic biology

U2 - 10.1039/d0sm02269a

DO - 10.1039/d0sm02269a

M3 - Article (Academic Journal)

C2 - 34231559

SN - 1744-683X

VL - 17

SP - 6873

EP - 6883

JO - Soft Matter

JF - Soft Matter

IS - 28

ER -

Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size

Abstract

Bibliographical note

Research Groups and Themes

Keywords

Access to Document

Handle.net

Fingerprint

Cite this