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

Paolo Bertoncello Orcid Logo

Protein Science

Swansea University Author: Paolo Bertoncello Orcid Logo

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
Published: Wiley
URI: https://cronfa.swan.ac.uk/Record/cronfa68578
first_indexed 2025-01-09T20:33:52Z
last_indexed 2025-01-09T20:33:52Z
id cronfa68578
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spelling 2024-12-17T12:38:36.1721525 v2 68578 2024-12-17 Chemical and temporal manipulation of early steps in protein assembly tune 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 Wiley protein-based materials, biomaterials, coacervation, aggregation, self-healing, phase separation, intrinsically disordered proteins 0 0 0 0001-01-01 COLLEGE NANME Engineering and Applied Sciences School COLLEGE CODE EAAS Swansea University 2024-12-17T12:38:36.1721525 2024-12-17T12:08:59.7603568 Faculty of Science and Engineering School of Engineering and Applied Sciences - Chemical Engineering Paolo Bertoncello 0000-0002-6557-7885 1
title Chemical and temporal manipulation of early steps in protein assembly tune the structure and intermolecular interactions of protein-based materials
spellingShingle Chemical and temporal manipulation of early steps in protein assembly tune the structure and intermolecular interactions of protein-based materials
Paolo Bertoncello
title_short Chemical and temporal manipulation of early steps in protein assembly tune the structure and intermolecular interactions of protein-based materials
title_full Chemical and temporal manipulation of early steps in protein assembly tune the structure and intermolecular interactions of protein-based materials
title_fullStr Chemical and temporal manipulation of early steps in protein assembly tune the structure and intermolecular interactions of protein-based materials
title_full_unstemmed Chemical and temporal manipulation of early steps in protein assembly tune the structure and intermolecular interactions of protein-based materials
title_sort Chemical and temporal manipulation of early steps in protein assembly tune 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 Paolo Bertoncello
format Journal article
container_title Protein Science
institution Swansea University
publisher Wiley
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
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 0
active_str 0
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 0001-01-01T20:50:11Z
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score 11.047609

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