Data_Sheet_1_Crystallin Fusion Proteins Improve the Thermal Properties of Hair.PDF
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.
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References
- https://doi.org//10.1016/j.preteyeres.2006.10.003
- https://doi.org//10.1021/bi9017076
- https://doi.org//10.1002/psc.923
- https://doi.org//10.1007/s10973-010-0691-2
- https://doi.org//10.1016/j.tca.2009.05.005
- https://doi.org//10.1002/pro.5560021002
- https://doi.org//10.1039/c7ra10461h
- https://doi.org//10.1016/j.colsurfb.2004.10.005
- https://doi.org//10.1002/dta.1648
- https://doi.org//10.1046/j.1523-1747.1998.00146.x
- https://doi.org//10.1038/s41598-018-33085-8
- https://doi.org//10.1016/j.colsurfb.2017.11.026
- https://doi.org//10.1021/acsami.8b10158
- https://doi.org//10.1016/S0079-6107(98)00032-7
- https://doi.org//10.1111/j.1745-7270.2007.00320.x
- https://doi.org//10.1074/jbc.M308203200
- https://doi.org//10.1007/s10973-005-0051-9
- https://doi.org//10.4172/21670951.1000133
- https://doi.org//10.1021/la9811665
- https://doi.org//10.1111/ics.12065
- https://doi.org//10.1016/j.clindermatol.2008.04.004
- https://doi.org//10.1016/S1350-9462(96)00018-3
- https://doi.org//10.1038/s41598-019-50283-0
- https://doi.org//10.1111/ics.12483
- https://doi.org//10.1177/004051757504501006
- https://doi.org//10.1038/315771a0
- https://doi.org//10.1016/S0022-2836(83)80232-0
- https://doi.org//10.1016/j.jmb.2011.06.007.The
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- Bioprocessing, Bioproduction and Bioproducts
- Industrial Biotechnology Diagnostics (incl. Biosensors)
- Industrial Microbiology (incl. Biofeedstocks)
- Industrial Molecular Engineering of Nucleic Acids and Proteins
- Industrial Biotechnology not elsewhere classified
- Medical Biotechnology Diagnostics (incl. Biosensors)
- Biological Engineering
- Regenerative Medicine (incl. Stem Cells and Tissue Engineering)
- Medical Biotechnology not elsewhere classified
- Agricultural Marine Biotechnology
- Biomaterials
- Biomechanical Engineering
- Biotechnology
- Biomarkers
- Biomedical Engineering not elsewhere classified
- Genetic Engineering
- Synthetic Biology
- Bioremediation
- Medical Molecular Engineering of Nucleic Acids and Proteins
