Crystallin Fusion Proteins Improve the Thermal Properties of Hair
Styling hair with straightening irons is a popular daily hair routine that significantly damage the hair keratin fiber due to the high temperature applied. In this study, we investigate the effect of two fusion proteins based on the human eye γD-crystallin conjugated with a keratin-based peptide (KP...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-10-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fbioe.2019.00298/full |
| _version_ | 1828402498305523712 |
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| author | Ana Tinoco José Gonçalves Carla Silva Artur Cavaco-Paulo Artur Ribeiro |
| author_facet | Ana Tinoco José Gonçalves Carla Silva Artur Cavaco-Paulo Artur Ribeiro |
| author_sort | Ana Tinoco |
| collection | DOAJ |
| description | Styling hair with straightening irons is a popular daily hair routine that significantly damage the hair keratin fiber due to the high temperature applied. In this study, we investigate the effect of two fusion proteins based on the human eye γD-crystallin conjugated with a keratin-based peptide (KP-Cryst Wt and KP-Cryst Mut) on hair exposed to thermal damage. The mutant form was designed to improve protein stability and promote interaction with the hair. Through the study, it was demonstrated the protection of Asian and Caucasian virgin hair's structure by the pretreatments with the KP-Cryst fusion proteins. After hair thermal exposure, a higher water content was quantified by TGA on the hair fibers pretreated with the fusion proteins (about 38% for the KP-Cryst Wt and 44% for the KP-Cryst Mut). Also, negligible alterations in hair fibers' stiffness were observed after iron application, demonstrating the proteins capacity to effectively prevent the conversion of keratin α-helix structure into β-sheets. The results proved the capacity of the fusion proteins to bind to hair and protect it against high temperatures', supporting the development of new formulations based on the KP-Cryst proteins. |
| first_indexed | 2024-12-10T10:01:09Z |
| format | Article |
| id | doaj.art-a19e763d9ce34d0a8f467bd1ab27ebd2 |
| institution | Directory Open Access Journal |
| issn | 2296-4185 |
| language | English |
| last_indexed | 2024-12-10T10:01:09Z |
| publishDate | 2019-10-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj.art-a19e763d9ce34d0a8f467bd1ab27ebd22022-12-22T01:53:21ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852019-10-01710.3389/fbioe.2019.00298489071Crystallin Fusion Proteins Improve the Thermal Properties of HairAna TinocoJosé GonçalvesCarla SilvaArtur Cavaco-PauloArtur RibeiroStyling hair with straightening irons is a popular daily hair routine that significantly damage the hair keratin fiber due to the high temperature applied. In this study, we investigate the effect of two fusion proteins based on the human eye γD-crystallin conjugated with a keratin-based peptide (KP-Cryst Wt and KP-Cryst Mut) on hair exposed to thermal damage. The mutant form was designed to improve protein stability and promote interaction with the hair. Through the study, it was demonstrated the protection of Asian and Caucasian virgin hair's structure by the pretreatments with the KP-Cryst fusion proteins. After hair thermal exposure, a higher water content was quantified by TGA on the hair fibers pretreated with the fusion proteins (about 38% for the KP-Cryst Wt and 44% for the KP-Cryst Mut). Also, negligible alterations in hair fibers' stiffness were observed after iron application, demonstrating the proteins capacity to effectively prevent the conversion of keratin α-helix structure into β-sheets. The results proved the capacity of the fusion proteins to bind to hair and protect it against high temperatures', supporting the development of new formulations based on the KP-Cryst proteins.https://www.frontiersin.org/article/10.3389/fbioe.2019.00298/fullproteinsγD-crystallinhairthermal damageprotectionkeratin-based peptide |
| spellingShingle | Ana Tinoco José Gonçalves Carla Silva Artur Cavaco-Paulo Artur Ribeiro Crystallin Fusion Proteins Improve the Thermal Properties of Hair Frontiers in Bioengineering and Biotechnology proteins γD-crystallin hair thermal damage protection keratin-based peptide |
| title | Crystallin Fusion Proteins Improve the Thermal Properties of Hair |
| title_full | Crystallin Fusion Proteins Improve the Thermal Properties of Hair |
| title_fullStr | Crystallin Fusion Proteins Improve the Thermal Properties of Hair |
| title_full_unstemmed | Crystallin Fusion Proteins Improve the Thermal Properties of Hair |
| title_short | Crystallin Fusion Proteins Improve the Thermal Properties of Hair |
| title_sort | crystallin fusion proteins improve the thermal properties of hair |
| topic | proteins γD-crystallin hair thermal damage protection keratin-based peptide |
| url | https://www.frontiersin.org/article/10.3389/fbioe.2019.00298/full |
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