Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material

Detalhes bibliográficos
Autor(a) principal: Volkov, Vadim
Data de Publicação: 2014
Outros Autores: Vasconcelos, Andreia, Sárria, M. P., Gomes, Andreia, Paulo, Artur Cavaco
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/31800
Resumo: Silk fibroin demonstrates great biocompatibility and is suitable for many biomedical applications, including tissue engineering and regenerative medicine. Current research focuses on manipulating the physico-chemical properties of fibroin, and examining the effect of this manipulation on firobin's biocompatibility. Regenerated silk fibroin was modified by in vitro enzymatic phosphorylation and cast into films. Films were produced by blending, at several ratios, the phosphorylated and un-phosphorylated fibroin solutions. Fourier transform infra-red spectroscopy was used to determine the specific P–OH vibration peak, confirming the phosphorylation of the regenerated silk fibroin solution. Differential scanning calorimetry showed that phosphorylation altered the intra- and inter-molecular interactions. Further experiments demonstrated that phosphorylation can be used to tailor the hydrophylicity/hydrophobicity ratio as well as the crystalinity of silk fibroin films. Release profiling of a model drug was highly dependent on silk modification level. Cytotoxicity assays showed that exposure to lixiviates of phosphorylated films only slightly affected cellular metabolism and proliferation, although direct contact resulted in a strong direct correlation between phosphorylation level and cell proliferation. This new method for tuning silk biomaterials to obtain specific structural and biochemical features can be adapted for a wide range of applications. Phosphorylation of silk fibroins may be applied to improve the cytocompatibility of any silk-based device that is considered to be in contact with live animals or human tissues.
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spelling Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable materialKinasesSilk fibroinSilk phosphorylationTextile biotechnologyScience & TechnologySilk fibroin demonstrates great biocompatibility and is suitable for many biomedical applications, including tissue engineering and regenerative medicine. Current research focuses on manipulating the physico-chemical properties of fibroin, and examining the effect of this manipulation on firobin's biocompatibility. Regenerated silk fibroin was modified by in vitro enzymatic phosphorylation and cast into films. Films were produced by blending, at several ratios, the phosphorylated and un-phosphorylated fibroin solutions. Fourier transform infra-red spectroscopy was used to determine the specific P–OH vibration peak, confirming the phosphorylation of the regenerated silk fibroin solution. Differential scanning calorimetry showed that phosphorylation altered the intra- and inter-molecular interactions. Further experiments demonstrated that phosphorylation can be used to tailor the hydrophylicity/hydrophobicity ratio as well as the crystalinity of silk fibroin films. Release profiling of a model drug was highly dependent on silk modification level. Cytotoxicity assays showed that exposure to lixiviates of phosphorylated films only slightly affected cellular metabolism and proliferation, although direct contact resulted in a strong direct correlation between phosphorylation level and cell proliferation. This new method for tuning silk biomaterials to obtain specific structural and biochemical features can be adapted for a wide range of applications. Phosphorylation of silk fibroins may be applied to improve the cytocompatibility of any silk-based device that is considered to be in contact with live animals or human tissues.The authors would like to acknowledge the support granted to the authors by European NOVO Project, contract no. FP7-HEALTH 2011-two-stage 278402.WileyUniversidade do MinhoVolkov, VadimVasconcelos, AndreiaSárria, M. P.Gomes, AndreiaPaulo, Artur Cavaco2014-102014-10-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/31800engVolkov, V.; Vasconcelos, Andreia; Sárria, M. P.; Gomes, Andreia C.; Paulo, Artur Cavaco, Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: A platform for the production of tuneable material. Biotechnology Journal, 9(10), 1267-1278, 20141860-67681860-731410.1002/biot.20140030225087614http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1860-7314info: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:RCAAP2023-07-21T11:57:34Zoai:repositorium.sdum.uminho.pt:1822/31800Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:47:13.953989Repositório 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 Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
title Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
spellingShingle Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
Volkov, Vadim
Kinases
Silk fibroin
Silk phosphorylation
Textile biotechnology
Science & Technology
title_short Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
title_full Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
title_fullStr Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
title_full_unstemmed Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
title_sort Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: a platform for the production of tuneable material
author Volkov, Vadim
author_facet Volkov, Vadim
Vasconcelos, Andreia
Sárria, M. P.
Gomes, Andreia
Paulo, Artur Cavaco
author_role author
author2 Vasconcelos, Andreia
Sárria, M. P.
Gomes, Andreia
Paulo, Artur Cavaco
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Volkov, Vadim
Vasconcelos, Andreia
Sárria, M. P.
Gomes, Andreia
Paulo, Artur Cavaco
dc.subject.por.fl_str_mv Kinases
Silk fibroin
Silk phosphorylation
Textile biotechnology
Science & Technology
topic Kinases
Silk fibroin
Silk phosphorylation
Textile biotechnology
Science & Technology
description Silk fibroin demonstrates great biocompatibility and is suitable for many biomedical applications, including tissue engineering and regenerative medicine. Current research focuses on manipulating the physico-chemical properties of fibroin, and examining the effect of this manipulation on firobin's biocompatibility. Regenerated silk fibroin was modified by in vitro enzymatic phosphorylation and cast into films. Films were produced by blending, at several ratios, the phosphorylated and un-phosphorylated fibroin solutions. Fourier transform infra-red spectroscopy was used to determine the specific P–OH vibration peak, confirming the phosphorylation of the regenerated silk fibroin solution. Differential scanning calorimetry showed that phosphorylation altered the intra- and inter-molecular interactions. Further experiments demonstrated that phosphorylation can be used to tailor the hydrophylicity/hydrophobicity ratio as well as the crystalinity of silk fibroin films. Release profiling of a model drug was highly dependent on silk modification level. Cytotoxicity assays showed that exposure to lixiviates of phosphorylated films only slightly affected cellular metabolism and proliferation, although direct contact resulted in a strong direct correlation between phosphorylation level and cell proliferation. This new method for tuning silk biomaterials to obtain specific structural and biochemical features can be adapted for a wide range of applications. Phosphorylation of silk fibroins may be applied to improve the cytocompatibility of any silk-based device that is considered to be in contact with live animals or human tissues.
publishDate 2014
dc.date.none.fl_str_mv 2014-10
2014-10-01T00:00:00Z
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/1822/31800
url http://hdl.handle.net/1822/31800
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Volkov, V.; Vasconcelos, Andreia; Sárria, M. P.; Gomes, Andreia C.; Paulo, Artur Cavaco, Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: A platform for the production of tuneable material. Biotechnology Journal, 9(10), 1267-1278, 2014
1860-6768
1860-7314
10.1002/biot.201400302
25087614
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1860-7314
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
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str 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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