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Spontaneous Coassembly of the Protein Terthiophene into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures
[Image: see text] Protein-based microfibers are biomaterials of paramount importance in materials science, nanotechnology, and medicine. Here we describe the spontaneous in situ formation and secretion of nanostructured protein microfibers in 2D and 3D cell cultures of 3T3 fibroblasts and B104 neuro...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9026133/ https://www.ncbi.nlm.nih.gov/pubmed/35474798 http://dx.doi.org/10.1021/acsomega.1c06677 |
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author | Palamà, Ilaria Elena Maiorano, Gabriele Di Maria, Francesca Zangoli, Mattia Candini, Andrea Zanelli, Alberto D’Amone, Stefania Fabiano, Eduardo Gigli, Giuseppe Barbarella, Giovanna |
author_facet | Palamà, Ilaria Elena Maiorano, Gabriele Di Maria, Francesca Zangoli, Mattia Candini, Andrea Zanelli, Alberto D’Amone, Stefania Fabiano, Eduardo Gigli, Giuseppe Barbarella, Giovanna |
author_sort | Palamà, Ilaria Elena |
collection | PubMed |
description | [Image: see text] Protein-based microfibers are biomaterials of paramount importance in materials science, nanotechnology, and medicine. Here we describe the spontaneous in situ formation and secretion of nanostructured protein microfibers in 2D and 3D cell cultures of 3T3 fibroblasts and B104 neuroblastoma cells upon treatment with a micromolar solution of either unmodified terthiophene or terthiophene modified by mono-oxygenation (thiophene → thiophene S-oxide) or dioxygenation (thiophene → thiophene S,S-dioxide) of the inner ring. We demonstrate via metabolic cytotoxicity tests that modification to the S-oxide leads to a severe drop in cell viability. By contrast, unmodified terthiophene and the respective S,S-dioxide cause no harm to the cells and lead to the formation and secretion of fluorescent and electroactive protein–fluorophore coassembled microfibers with a large aspect ratio, a micrometer-sized length and width, and a nanometer-sized thickness, as monitored in real-time by laser scanning confocal microscopy (LSCM). With respect to the microfibers formed by unmodified terthiophene, those formed by the S,S-dioxide display markedly red-shifted fluorescence and an increased n-type character of the material, as shown by macroscopic Kelvin probe in agreement with cyclovoltammetry data. Electrophoretic analyses and Q-TOF mass spectrometry of the isolated microfibers indicate that in all cases the prevalent proteins present are vimentin and histone H4, thus revealing the capability of these fluorophores to selectively coassemble with these proteins. Finally, DFT calculations help to illuminate the fluorophore–fluorophore intermolecular interactions contributing to the formation of the microfibers. |
format | Online Article Text |
id | pubmed-9026133 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-90261332022-04-25 Spontaneous Coassembly of the Protein Terthiophene into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures Palamà, Ilaria Elena Maiorano, Gabriele Di Maria, Francesca Zangoli, Mattia Candini, Andrea Zanelli, Alberto D’Amone, Stefania Fabiano, Eduardo Gigli, Giuseppe Barbarella, Giovanna ACS Omega [Image: see text] Protein-based microfibers are biomaterials of paramount importance in materials science, nanotechnology, and medicine. Here we describe the spontaneous in situ formation and secretion of nanostructured protein microfibers in 2D and 3D cell cultures of 3T3 fibroblasts and B104 neuroblastoma cells upon treatment with a micromolar solution of either unmodified terthiophene or terthiophene modified by mono-oxygenation (thiophene → thiophene S-oxide) or dioxygenation (thiophene → thiophene S,S-dioxide) of the inner ring. We demonstrate via metabolic cytotoxicity tests that modification to the S-oxide leads to a severe drop in cell viability. By contrast, unmodified terthiophene and the respective S,S-dioxide cause no harm to the cells and lead to the formation and secretion of fluorescent and electroactive protein–fluorophore coassembled microfibers with a large aspect ratio, a micrometer-sized length and width, and a nanometer-sized thickness, as monitored in real-time by laser scanning confocal microscopy (LSCM). With respect to the microfibers formed by unmodified terthiophene, those formed by the S,S-dioxide display markedly red-shifted fluorescence and an increased n-type character of the material, as shown by macroscopic Kelvin probe in agreement with cyclovoltammetry data. Electrophoretic analyses and Q-TOF mass spectrometry of the isolated microfibers indicate that in all cases the prevalent proteins present are vimentin and histone H4, thus revealing the capability of these fluorophores to selectively coassemble with these proteins. Finally, DFT calculations help to illuminate the fluorophore–fluorophore intermolecular interactions contributing to the formation of the microfibers. American Chemical Society 2022-04-06 /pmc/articles/PMC9026133/ /pubmed/35474798 http://dx.doi.org/10.1021/acsomega.1c06677 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Palamà, Ilaria Elena Maiorano, Gabriele Di Maria, Francesca Zangoli, Mattia Candini, Andrea Zanelli, Alberto D’Amone, Stefania Fabiano, Eduardo Gigli, Giuseppe Barbarella, Giovanna Spontaneous Coassembly of the Protein Terthiophene into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures |
title | Spontaneous Coassembly of the Protein Terthiophene
into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures |
title_full | Spontaneous Coassembly of the Protein Terthiophene
into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures |
title_fullStr | Spontaneous Coassembly of the Protein Terthiophene
into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures |
title_full_unstemmed | Spontaneous Coassembly of the Protein Terthiophene
into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures |
title_short | Spontaneous Coassembly of the Protein Terthiophene
into Fluorescent Electroactive Microfibers in 2D and 3D Cell Cultures |
title_sort | spontaneous coassembly of the protein terthiophene
into fluorescent electroactive microfibers in 2d and 3d cell cultures |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9026133/ https://www.ncbi.nlm.nih.gov/pubmed/35474798 http://dx.doi.org/10.1021/acsomega.1c06677 |
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