Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/25932 |
Resumo: | The objective of this work was to develop a new strategy to physically ‘repair’ chemically damaged hair. Hence the human eye γD-crystallin, a protein from the superfamily characterized structurally by the Greek key motif, was studied. The human γD-crystallin was chosen based on the ability of proteins belonging to this superfamily to be involved in the coating of specific structures. Two crystallins were used on the study, the wild type (Protein Data Bank ID: 1HK0) and the mutant protein. The mutant form was intended to induce a strong and quick protein polymerization as well to have new possible points of anchorage to hair. |
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Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibilityGreek key motifHair treatmentHuman crystallinMechanical properties improvementOver bleached hairScience & TechnologyThe objective of this work was to develop a new strategy to physically ‘repair’ chemically damaged hair. Hence the human eye γD-crystallin, a protein from the superfamily characterized structurally by the Greek key motif, was studied. The human γD-crystallin was chosen based on the ability of proteins belonging to this superfamily to be involved in the coating of specific structures. Two crystallins were used on the study, the wild type (Protein Data Bank ID: 1HK0) and the mutant protein. The mutant form was intended to induce a strong and quick protein polymerization as well to have new possible points of anchorage to hair.L'objectif de ce travail était de développer une nouvelle stratégie pour physiquement “réparer” les cheveux chimiquement endommagés. La protéine humaine γD-cristalline, une protéine de la superfamille caractérisée structurellement par le motif clé grecque, a été étudiée. Le γD-cristallin humain a été choisi en fonction de la capacité des protéines appartenant à cette superfamille d'être impliquées dans le revêtement des structures spécifiques. Deux cristallins ont été utilisés dans l'étude, le type sauvage (Protein Data Bank ID: 1HK0) et la protéine mutante. La forme mutante était destinée à induire une polymérisation de la protéine, forte et rapide ainsi d'avoir de nouveaux points d'ancrage possibles aux cheveux.This work is supported by FEDER through POFC-COMPETE and by national funds from FCT through the project PEst-C/BIA/UI4050/2011.WileyUniversidade do MinhoRibeiro, Artur J.Matamá, Maria TeresaCruz, Célia F.Gomes, A. C.Paulo, Artur Cavaco20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/25932eng1468-249410.1111/ics.1206523651449http://dx.doi.org/10.1111/ics.12065info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:09:56Zoai:repositorium.sdum.uminho.pt:1822/25932Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:01:28.201892Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility |
title |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility |
spellingShingle |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility Ribeiro, Artur J. Greek key motif Hair treatment Human crystallin Mechanical properties improvement Over bleached hair Science & Technology |
title_short |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility |
title_full |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility |
title_fullStr |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility |
title_full_unstemmed |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility |
title_sort |
Potential of human γD-crystallin for hair damage repair : insights into the mechanical properties and biocompatibility |
author |
Ribeiro, Artur J. |
author_facet |
Ribeiro, Artur J. Matamá, Maria Teresa Cruz, Célia F. Gomes, A. C. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Matamá, Maria Teresa Cruz, Célia F. Gomes, A. C. Paulo, Artur Cavaco |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Ribeiro, Artur J. Matamá, Maria Teresa Cruz, Célia F. Gomes, A. C. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Greek key motif Hair treatment Human crystallin Mechanical properties improvement Over bleached hair Science & Technology |
topic |
Greek key motif Hair treatment Human crystallin Mechanical properties improvement Over bleached hair Science & Technology |
description |
The objective of this work was to develop a new strategy to physically ‘repair’ chemically damaged hair. Hence the human eye γD-crystallin, a protein from the superfamily characterized structurally by the Greek key motif, was studied. The human γD-crystallin was chosen based on the ability of proteins belonging to this superfamily to be involved in the coating of specific structures. Two crystallins were used on the study, the wild type (Protein Data Bank ID: 1HK0) and the mutant protein. The mutant form was intended to induce a strong and quick protein polymerization as well to have new possible points of anchorage to hair. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 2013-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/1822/25932 |
url |
http://hdl.handle.net/1822/25932 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1468-2494 10.1111/ics.12065 23651449 http://dx.doi.org/10.1111/ics.12065 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Wiley |
publisher.none.fl_str_mv |
Wiley |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799132413133062144 |