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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...

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Autores principales: Tinoco, Ana, Antunes, Egipto, Martins, Madalena, Gonçalves, Filipa, Gomes, Andreia C., Silva, Carla, Cavaco-Paulo, Artur, Ribeiro, Artur
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
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.
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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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