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Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability
Hybrid protein nanofibers (hPNFs) have been identified as promising nano building blocks for numerous applications in nanomedicine and tissue engineering. We have recently reported a nature-inspired, self-assembly route to create hPNFs from human plasma proteins, i.e., albumin and hemoglobin. Howeve...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8697752/ https://www.ncbi.nlm.nih.gov/pubmed/35423936 http://dx.doi.org/10.1039/d0ra10749b |
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author | Scheuer, Karl Helbing, Christian Firkowska-Boden, Izabela Jandt, Klaus D. |
author_facet | Scheuer, Karl Helbing, Christian Firkowska-Boden, Izabela Jandt, Klaus D. |
author_sort | Scheuer, Karl |
collection | PubMed |
description | Hybrid protein nanofibers (hPNFs) have been identified as promising nano building blocks for numerous applications in nanomedicine and tissue engineering. We have recently reported a nature-inspired, self-assembly route to create hPNFs from human plasma proteins, i.e., albumin and hemoglobin. However, it is still unclear whether the same route can be applied to other plasma proteins and whether it is possible to control the composition of the resulting fibers. In this context, to further understand the hPNFs self-assembly mechanism and to optimize their properties, we report herein on ethanol-induced self-assembly of two different plasma proteins, i.e., fibrinogen (FG) and fibronectin (FN). We show that by varying initial protein ratios, the composition and thus the properties of the resulting hPNFs can be fine-tuned. Specifically, atomic force microscopy, hydrodynamic diameter, and zeta potential data together revealed a strong correlation of the hPNFs dimensions and surface charge to their initial protein mixing ratio. The composition-independent prompt dissolution of hPNFs in ultrapure water, in contrast to their stability in PBS, indicates that the molecular arrangement of FN and FG in hPNFs is mainly based on electrostatic interactions. Supported by experimental data we introduce a feasible mechanism that explains the interactions between FN and FG and their self-assembly to hPNFs. These findings contribute to the understanding of dual protein interactions, which can be beneficial in designing innovative biomaterials with multifaceted biological and physical characteristics. |
format | Online Article Text |
id | pubmed-8697752 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-86977522022-04-13 Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability Scheuer, Karl Helbing, Christian Firkowska-Boden, Izabela Jandt, Klaus D. RSC Adv Chemistry Hybrid protein nanofibers (hPNFs) have been identified as promising nano building blocks for numerous applications in nanomedicine and tissue engineering. We have recently reported a nature-inspired, self-assembly route to create hPNFs from human plasma proteins, i.e., albumin and hemoglobin. However, it is still unclear whether the same route can be applied to other plasma proteins and whether it is possible to control the composition of the resulting fibers. In this context, to further understand the hPNFs self-assembly mechanism and to optimize their properties, we report herein on ethanol-induced self-assembly of two different plasma proteins, i.e., fibrinogen (FG) and fibronectin (FN). We show that by varying initial protein ratios, the composition and thus the properties of the resulting hPNFs can be fine-tuned. Specifically, atomic force microscopy, hydrodynamic diameter, and zeta potential data together revealed a strong correlation of the hPNFs dimensions and surface charge to their initial protein mixing ratio. The composition-independent prompt dissolution of hPNFs in ultrapure water, in contrast to their stability in PBS, indicates that the molecular arrangement of FN and FG in hPNFs is mainly based on electrostatic interactions. Supported by experimental data we introduce a feasible mechanism that explains the interactions between FN and FG and their self-assembly to hPNFs. These findings contribute to the understanding of dual protein interactions, which can be beneficial in designing innovative biomaterials with multifaceted biological and physical characteristics. The Royal Society of Chemistry 2021-04-16 /pmc/articles/PMC8697752/ /pubmed/35423936 http://dx.doi.org/10.1039/d0ra10749b Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Scheuer, Karl Helbing, Christian Firkowska-Boden, Izabela Jandt, Klaus D. Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability |
title | Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability |
title_full | Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability |
title_fullStr | Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability |
title_full_unstemmed | Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability |
title_short | Self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability |
title_sort | self-assembled fibrinogen–fibronectin hybrid protein nanofibers with medium-sensitive stability |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8697752/ https://www.ncbi.nlm.nih.gov/pubmed/35423936 http://dx.doi.org/10.1039/d0ra10749b |
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