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Fusion proteins with chromogenic and keratin binding modules
The present research relates to a fusion protein comprising a chromogenic blue ultramarine protein (UM) bound to a keratin-based peptide (KP). The KP-UM fusion protein explores UM chromogenic nature together with KP affinity towards hair. For the first time a fusion protein with a chromogenic nature...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6773707/ https://www.ncbi.nlm.nih.gov/pubmed/31575960 http://dx.doi.org/10.1038/s41598-019-50283-0 |
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author | Tinoco, Ana Antunes, Egipto Martins, Madalena Gonçalves, Filipa Gomes, Andreia C. Silva, Carla Cavaco-Paulo, Artur Ribeiro, Artur |
author_facet | Tinoco, Ana Antunes, Egipto Martins, Madalena Gonçalves, Filipa Gomes, Andreia C. Silva, Carla Cavaco-Paulo, Artur Ribeiro, Artur |
author_sort | Tinoco, Ana |
collection | PubMed |
description | The present research relates to a fusion protein comprising a chromogenic blue ultramarine protein (UM) bound to a keratin-based peptide (KP). The KP-UM fusion protein explores UM chromogenic nature together with KP affinity towards hair. For the first time a fusion protein with a chromogenic nature is explored as a hair coloring agent. The KP-UM protein colored overbleached hair, being the color dependent on the formulation polarity. The protein was able to bind to the hair cuticle and even to penetrate throughout the hair fibre. Molecular dynamics studies demonstrated that the interaction between the KP-UM protein and the hair was mediated by the KP sequence. All the formulations recovered the mechanical properties of overbleached hair and KP-UM proved to be safe when tested in human keratinocytes. Although based on a chromogenic non-fluorescent protein, the KP-UM protein presented a photoswitch phenomenon, changing from chromogenic to fluorescent depending on the wavelength selected for excitation. KP-UM protein shows the potential to be incorporated in new eco-friendly cosmetic formulations for hair coloration, decreasing the use of traditional dyes and reducing its environmental impact. |
format | Online Article Text |
id | pubmed-6773707 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-67737072019-10-04 Fusion proteins with chromogenic and keratin binding modules Tinoco, Ana Antunes, Egipto Martins, Madalena Gonçalves, Filipa Gomes, Andreia C. Silva, Carla Cavaco-Paulo, Artur Ribeiro, Artur Sci Rep Article The present research relates to a fusion protein comprising a chromogenic blue ultramarine protein (UM) bound to a keratin-based peptide (KP). The KP-UM fusion protein explores UM chromogenic nature together with KP affinity towards hair. For the first time a fusion protein with a chromogenic nature is explored as a hair coloring agent. The KP-UM protein colored overbleached hair, being the color dependent on the formulation polarity. The protein was able to bind to the hair cuticle and even to penetrate throughout the hair fibre. Molecular dynamics studies demonstrated that the interaction between the KP-UM protein and the hair was mediated by the KP sequence. All the formulations recovered the mechanical properties of overbleached hair and KP-UM proved to be safe when tested in human keratinocytes. Although based on a chromogenic non-fluorescent protein, the KP-UM protein presented a photoswitch phenomenon, changing from chromogenic to fluorescent depending on the wavelength selected for excitation. KP-UM protein shows the potential to be incorporated in new eco-friendly cosmetic formulations for hair coloration, decreasing the use of traditional dyes and reducing its environmental impact. Nature Publishing Group UK 2019-10-01 /pmc/articles/PMC6773707/ /pubmed/31575960 http://dx.doi.org/10.1038/s41598-019-50283-0 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Tinoco, Ana Antunes, Egipto Martins, Madalena Gonçalves, Filipa Gomes, Andreia C. Silva, Carla Cavaco-Paulo, Artur Ribeiro, Artur Fusion proteins with chromogenic and keratin binding modules |
title | Fusion proteins with chromogenic and keratin binding modules |
title_full | Fusion proteins with chromogenic and keratin binding modules |
title_fullStr | Fusion proteins with chromogenic and keratin binding modules |
title_full_unstemmed | Fusion proteins with chromogenic and keratin binding modules |
title_short | Fusion proteins with chromogenic and keratin binding modules |
title_sort | fusion proteins with chromogenic and keratin binding modules |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6773707/ https://www.ncbi.nlm.nih.gov/pubmed/31575960 http://dx.doi.org/10.1038/s41598-019-50283-0 |
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