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Health improvement of human hair and their reshaping using recombinant keratin K31

Hair, being one of the most important components of the beauty care processes, attracts the use of a variety of hair treating cosmetics. Conventional hair treating cosmetics are not satisfactory for one reason or the other. Commercially used keratins are isolated from wool or chicken feathers. As th...

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Detalles Bibliográficos
Autores principales: Basit, Abdul, asghar, Faiza, Sadaf, Saima, Akhtar, M. Waheed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6218806/
https://www.ncbi.nlm.nih.gov/pubmed/30416979
http://dx.doi.org/10.1016/j.btre.2018.e00288
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author Basit, Abdul
asghar, Faiza
Sadaf, Saima
Akhtar, M. Waheed
author_facet Basit, Abdul
asghar, Faiza
Sadaf, Saima
Akhtar, M. Waheed
author_sort Basit, Abdul
collection PubMed
description Hair, being one of the most important components of the beauty care processes, attracts the use of a variety of hair treating cosmetics. Conventional hair treating cosmetics are not satisfactory for one reason or the other. Commercially used keratins are isolated from wool or chicken feathers. As these lack complete sequence identity with human hair keratin, are likely to be less efficient than the human hair keratin. K31, a type I acidic keratin, is a major protein of human hair keratin complex and it is essential for maintaining the hair tensile strength. In this study keratin K31 (46 kDa) gene was expressed in Escherichia coli at a level of approximately 35% of the total cell proteins. The protein, however, was expressed as insoluble inclusion bodies. The expressed protein was refolded and purified by FPLC using an anion-exchange column. The CD analysis results showed that the K31 was properly refolded. MALDI-TOF mass spectroscopy showed the characteristics expected for human K31 keratin. The refolded and partially purified K31 protein, when applied on chemically damaged hairs, increased the diameter of the hair up to 49%. The mechanical strength of the bleached hair increased by almost 2 fold after a single treatment of K31. The protein also straightened curly hair efficiently on a single treatment for one hour. Application of K31 resulted in marked improvements in smoothness, diameter and mechanical strength of the damaged hair.
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spelling pubmed-62188062018-11-09 Health improvement of human hair and their reshaping using recombinant keratin K31 Basit, Abdul asghar, Faiza Sadaf, Saima Akhtar, M. Waheed Biotechnol Rep (Amst) Article Hair, being one of the most important components of the beauty care processes, attracts the use of a variety of hair treating cosmetics. Conventional hair treating cosmetics are not satisfactory for one reason or the other. Commercially used keratins are isolated from wool or chicken feathers. As these lack complete sequence identity with human hair keratin, are likely to be less efficient than the human hair keratin. K31, a type I acidic keratin, is a major protein of human hair keratin complex and it is essential for maintaining the hair tensile strength. In this study keratin K31 (46 kDa) gene was expressed in Escherichia coli at a level of approximately 35% of the total cell proteins. The protein, however, was expressed as insoluble inclusion bodies. The expressed protein was refolded and purified by FPLC using an anion-exchange column. The CD analysis results showed that the K31 was properly refolded. MALDI-TOF mass spectroscopy showed the characteristics expected for human K31 keratin. The refolded and partially purified K31 protein, when applied on chemically damaged hairs, increased the diameter of the hair up to 49%. The mechanical strength of the bleached hair increased by almost 2 fold after a single treatment of K31. The protein also straightened curly hair efficiently on a single treatment for one hour. Application of K31 resulted in marked improvements in smoothness, diameter and mechanical strength of the damaged hair. Elsevier 2018-10-24 /pmc/articles/PMC6218806/ /pubmed/30416979 http://dx.doi.org/10.1016/j.btre.2018.e00288 Text en © 2018 Published by Elsevier B.V. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Basit, Abdul
asghar, Faiza
Sadaf, Saima
Akhtar, M. Waheed
Health improvement of human hair and their reshaping using recombinant keratin K31
title Health improvement of human hair and their reshaping using recombinant keratin K31
title_full Health improvement of human hair and their reshaping using recombinant keratin K31
title_fullStr Health improvement of human hair and their reshaping using recombinant keratin K31
title_full_unstemmed Health improvement of human hair and their reshaping using recombinant keratin K31
title_short Health improvement of human hair and their reshaping using recombinant keratin K31
title_sort health improvement of human hair and their reshaping using recombinant keratin k31
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6218806/
https://www.ncbi.nlm.nih.gov/pubmed/30416979
http://dx.doi.org/10.1016/j.btre.2018.e00288
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