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Understanding novel EGFP-Ubx protein-based film formation / VALERIA ITALIA

Swansea University Author: VALERIA ITALIA

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DOI (Published version): 10.23889/SUthesis.59805

Abstract

Protein-based materials are currently the subject of intense research interest since they have an extended range of potential applications, such as im-proved bio-membrane biocompatibility for implanted medical devices and the creation of platform materials for novel biosensors. Monomers from Ultrabi...

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Published: Swansea 2022
Institution: Swansea University
Degree level: Doctoral
Degree name: Ph.D
Supervisor: Meissner, Kenith E. ; Bertoncello, Paolo ; Martin, Donald ; Maccarini, Marco
URI: https://cronfa.swan.ac.uk/Record/cronfa59805
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first_indexed 2022-04-12T13:48:13Z
last_indexed 2022-04-13T03:32:53Z
id cronfa59805
recordtype RisThesis
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spelling 2022-04-12T15:29:08.1507974 v2 59805 2022-04-12 Understanding novel EGFP-Ubx protein-based film formation 609166e00715a81ea1104ecec3599e89 VALERIA ITALIA VALERIA ITALIA true false 2022-04-12 Protein-based materials are currently the subject of intense research interest since they have an extended range of potential applications, such as im-proved bio-membrane biocompatibility for implanted medical devices and the creation of platform materials for novel biosensors. Monomers from Ultrabithorax (Ubx) transcription factor are known to spontaneously self-assemble at an air-water interface to form a monolayer, which has then been used as a basis for forming biopolymeric ˝bers. Here we used the Lang-muir trough technique, Brewster angle microscopy (BAM), ellipsometry and neutron re˛ectometry (NR) to investigate the in˛uences of di˙erent exper-imental conditions on EGFP-Ubx monolayer formation and the impact on biopolymeric ˝ber structure. We varied protein concentration, bu˙er prop-erties and waiting times prior to forming biopolymeric ˝bers. Interestingly, we found 3 phases of material formation which brought us to a new protocol for forming ˝bers that reduced protein concentration by 5-fold and wait-ing times by 100-fold. Moreover, an in-house developed MATLAB code was used to analyze SEM images and obtain quantitative structural information about the biopolymeric ˝bers that were correlated directly to the surface ˝lm characteristics measured in the LB trough. These new insights into ˝ber formation and structure enhance the usefulness of the Ubx-based biopolymer for biomedical applications. E-Thesis Swansea Protein, neutron reflectometry, Langmuir trough, biopolymer 8 4 2022 2022-04-08 10.23889/SUthesis.59805 COLLEGE NANME COLLEGE CODE Swansea University Meissner, Kenith E. ; Bertoncello, Paolo ; Martin, Donald ; Maccarini, Marco Doctoral Ph.D 2022-04-12T15:29:08.1507974 2022-04-12T14:33:04.6577329 Faculty of Science and Engineering School of Biosciences, Geography and Physics - Physics VALERIA ITALIA 1 59805__23817__9a76ed9c0d9e4eb7a3a13a7f4e33aedd.pdf Italia_Valeria_PhD_Thesis_Final_Redacted_Signature.pdf 2022-04-12T14:58:18.2658768 Output 19079026 application/pdf E-Thesis – open access true Copyright: The author, Valeria Italia, 2022. true eng
title Understanding novel EGFP-Ubx protein-based film formation
spellingShingle Understanding novel EGFP-Ubx protein-based film formation
VALERIA ITALIA
title_short Understanding novel EGFP-Ubx protein-based film formation
title_full Understanding novel EGFP-Ubx protein-based film formation
title_fullStr Understanding novel EGFP-Ubx protein-based film formation
title_full_unstemmed Understanding novel EGFP-Ubx protein-based film formation
title_sort Understanding novel EGFP-Ubx protein-based film formation
author_id_str_mv 609166e00715a81ea1104ecec3599e89
author_id_fullname_str_mv 609166e00715a81ea1104ecec3599e89_***_VALERIA ITALIA
author VALERIA ITALIA
author2 VALERIA ITALIA
format E-Thesis
publishDate 2022
institution Swansea University
doi_str_mv 10.23889/SUthesis.59805
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 Biosciences, Geography and Physics - Physics{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Biosciences, Geography and Physics - Physics
document_store_str 1
active_str 0
description Protein-based materials are currently the subject of intense research interest since they have an extended range of potential applications, such as im-proved bio-membrane biocompatibility for implanted medical devices and the creation of platform materials for novel biosensors. Monomers from Ultrabithorax (Ubx) transcription factor are known to spontaneously self-assemble at an air-water interface to form a monolayer, which has then been used as a basis for forming biopolymeric ˝bers. Here we used the Lang-muir trough technique, Brewster angle microscopy (BAM), ellipsometry and neutron re˛ectometry (NR) to investigate the in˛uences of di˙erent exper-imental conditions on EGFP-Ubx monolayer formation and the impact on biopolymeric ˝ber structure. We varied protein concentration, bu˙er prop-erties and waiting times prior to forming biopolymeric ˝bers. Interestingly, we found 3 phases of material formation which brought us to a new protocol for forming ˝bers that reduced protein concentration by 5-fold and wait-ing times by 100-fold. Moreover, an in-house developed MATLAB code was used to analyze SEM images and obtain quantitative structural information about the biopolymeric ˝bers that were correlated directly to the surface ˝lm characteristics measured in the LB trough. These new insights into ˝ber formation and structure enhance the usefulness of the Ubx-based biopolymer for biomedical applications.
published_date 2022-04-08T04:17:23Z
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score 11.036116

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