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Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials

Valeria Italia, Amanda Jons, Bhavika Kaparthi, Britt Faulk, Marco Maccarini, Paolo Bertoncello Orcid Logo, Ken Meissner, Donald K. Martin Orcid Logo, Sarah E. Bondos Orcid Logo

Protein Science, Volume: 34, Issue: 2

Swansea University Author: Paolo Bertoncello Orcid Logo

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DOI (Published version): 10.1002/pro.70000

Abstract

The Drosophila intrinsically disordered protein Ultrabithorax (Ubx) undergoes a series of phase transitions, beginning with noncovalent interactions between apparently randomly organized monomers, and evolving over time to form increasingly ordered coacervates. This assembly process ends when specif...

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Published in: Protein Science
ISSN: 0961-8368 1469-896X
Published: Wiley 2025
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URI: https://cronfa.swan.ac.uk/Record/cronfa68578
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spelling v2 68578 2024-12-17 Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials ad352842aa5fe9c1947bd24ff61816c8 0000-0002-6557-7885 Paolo Bertoncello Paolo Bertoncello true false 2024-12-17 EAAS The Drosophila intrinsically disordered protein Ultrabithorax (Ubx) undergoes a series of phase transitions, beginning with noncovalent interactions between apparently randomly organized monomers, and evolving over time to form increasingly ordered coacervates. This assembly process ends when specific dityrosine covalent bonds lock the monomers in place, forming macroscale materials. Inspired by this hierarchical, multi-step assembly process, we analyzed the impact of protein concentration, assembly time, and subphase composition on the early, noncovalent stages of Ubx assembly, which are extremely sensitive to their environment. We discovered that in low salt buffers, we can generate a new type of Ubx material from early coacervates using 5-fold less protein, and 100-fold less assembly time. Comparison of the new materials with standard Ubx fibers also revealed differences in the extent of wrinkling on the fiber surface. A new image analysis technique based on autocorrelation of Scanning Electron Microscopy (SEM) images was developed to quantify these structural differences. These differences extend to the molecular level: new materials form more dityrosine covalent cross-links per monomer, but without requiring the specific tyrosine residues necessary for crosslinking previously established materials. We conclude that varying the assembly conditions represents a facile and inexpensive process for creating new materials. Most new biopolymers are created by changing the composition of the monomers or the method used to drive assembly. In contrast, in this study we used the same monomers and assembly approach, but altered the assembly time and chemical environment to create a new material with unique properties. Journal Article Protein Science 34 2 Wiley 0961-8368 1469-896X protein-based materials, biomaterials, coacervation, aggregation, self-healing, phase separation, intrinsically disordered proteins 1 2 2025 2025-02-01 10.1002/pro.70000 COLLEGE NANME Engineering and Applied Sciences School COLLEGE CODE EAAS Swansea University VI was funded by a Cotutelle Fellowship from the ubBIO project, funded by the IDEX Strategic Alliance between University Grenoble Alpes (France) and Swansea University (UK). 2025-01-23T10:31:43.4613554 2024-12-17T12:08:59.7603568 Faculty of Science and Engineering School of Engineering and Applied Sciences - Chemical Engineering Valeria Italia 1 Amanda Jons 2 Bhavika Kaparthi 3 Britt Faulk 4 Marco Maccarini 5 Paolo Bertoncello 0000-0002-6557-7885 6 Ken Meissner 7 Donald K. Martin 0000-0001-5913-2372 8 Sarah E. Bondos 0000-0002-9673-4169 9 68578__33158__3eeeb5dc492b431fb44bc800dd245521.pdf 68578.AAM.pdf 2024-12-17T12:12:47.5184660 Output 1105422 application/pdf Accepted Manuscript true Author accepted manuscript document released under the terms of a Creative Commons CC-BY licence using the Swansea University Research Publications Policy (rights retention). true eng https://creativecommons.org/licenses/by/4.0/deed.en 68578__33159__91476c9492a74a218b8b16f36be21e30.pdf 68578.Supplemental.Materials.pdf 2024-12-17T12:13:03.9291229 Output 266728 application/pdf Supplemental material true Document released under the terms of a Creative Commons CC-BY licence using the Swansea University Research Publications Policy (rights retention). true eng https://creativecommons.org/licenses/by/4.0/deed.en
title Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials
spellingShingle Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials
Paolo Bertoncello
title_short Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials
title_full Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials
title_fullStr Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials
title_full_unstemmed Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials
title_sort Chemical and temporal manipulation of early steps in protein assembly tunes the structure and intermolecular interactions of protein‐based materials
author_id_str_mv ad352842aa5fe9c1947bd24ff61816c8
author_id_fullname_str_mv ad352842aa5fe9c1947bd24ff61816c8_***_Paolo Bertoncello
author Paolo Bertoncello
author2 Valeria Italia
Amanda Jons
Bhavika Kaparthi
Britt Faulk
Marco Maccarini
Paolo Bertoncello
Ken Meissner
Donald K. Martin
Sarah E. Bondos
format Journal article
container_title Protein Science
container_volume 34
container_issue 2
publishDate 2025
institution Swansea University
issn 0961-8368
1469-896X
doi_str_mv 10.1002/pro.70000
publisher Wiley
college_str Faculty of Science and Engineering
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hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Engineering and Applied Sciences - Chemical Engineering{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Engineering and Applied Sciences - Chemical Engineering
document_store_str 1
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description The Drosophila intrinsically disordered protein Ultrabithorax (Ubx) undergoes a series of phase transitions, beginning with noncovalent interactions between apparently randomly organized monomers, and evolving over time to form increasingly ordered coacervates. This assembly process ends when specific dityrosine covalent bonds lock the monomers in place, forming macroscale materials. Inspired by this hierarchical, multi-step assembly process, we analyzed the impact of protein concentration, assembly time, and subphase composition on the early, noncovalent stages of Ubx assembly, which are extremely sensitive to their environment. We discovered that in low salt buffers, we can generate a new type of Ubx material from early coacervates using 5-fold less protein, and 100-fold less assembly time. Comparison of the new materials with standard Ubx fibers also revealed differences in the extent of wrinkling on the fiber surface. A new image analysis technique based on autocorrelation of Scanning Electron Microscopy (SEM) images was developed to quantify these structural differences. These differences extend to the molecular level: new materials form more dityrosine covalent cross-links per monomer, but without requiring the specific tyrosine residues necessary for crosslinking previously established materials. We conclude that varying the assembly conditions represents a facile and inexpensive process for creating new materials. Most new biopolymers are created by changing the composition of the monomers or the method used to drive assembly. In contrast, in this study we used the same monomers and assembly approach, but altered the assembly time and chemical environment to create a new material with unique properties.
published_date 2025-02-01T10:31:45Z
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