Fish sarcoplasmic proteins as a high value marine material for wound dressing applications
Autor(a) principal: | |
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Data de Publicação: | 2018 |
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/1822/56290 |
Resumo: | Fish sarcoplasmic proteins (FSP) constitute around 25–30% of the total fish muscle protein. As the FSP are water soluble, FSP were isolated from fresh cod (Gadus morhua) by centrifugation. By SDS-PAGE, it was possible to determine the composition of FSP extracts (FSP-E). The FSP-E undergo denaturation at 44.12 ± 2.34° C, as characterized by differential scanning calorimetry thermograms (DSC). The secondary structure of FSP-E is mainly composed by α-helix structure, as determined by circular dichroism. The cytocompatibility of FSP-E, at concentrations ranging from 5 to 20 mg/mL, was investigated. Concentrations lower than 10 mg/mL have no cytotoxicity cultures of fibroblasts over 72 h. Further on, FSP membranes (FSP-M) were produced by spin coating to evaluate its properties. FSP-M shown having uniform surface as analyzed by Scanning Electron Microscopy (SEM). The relative amount of α-helix structures is higher when compared with the FSP-E. The FSP-M have higher temperature stability than the FSP-E, since they presented a denaturation temperature of 58.88 ± 3.36° C, according to the DSC analysis. FSP-M shown distinctive mechanical properties, with a stiffness of 16.57 ± 3.95 MPa and a yield strength of 23.85 ± 5.97 MPa. Human lung fibroblasts cell lines (MRC-5) were cultured in direct contact with FSP-M, demonstrating its cytocompatibility for 48 h. Based on these results, FSP can be considered a potential biomaterial recovered from nature, for wound dressing applications. |
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Fish sarcoplasmic proteins as a high value marine material for wound dressing applicationsCytocompatibilitymembranesPhysico-chemical characterizationSarcoplasmic proteinsSpin coatingScience & TechnologyFish sarcoplasmic proteins (FSP) constitute around 25–30% of the total fish muscle protein. As the FSP are water soluble, FSP were isolated from fresh cod (Gadus morhua) by centrifugation. By SDS-PAGE, it was possible to determine the composition of FSP extracts (FSP-E). The FSP-E undergo denaturation at 44.12 ± 2.34° C, as characterized by differential scanning calorimetry thermograms (DSC). The secondary structure of FSP-E is mainly composed by α-helix structure, as determined by circular dichroism. The cytocompatibility of FSP-E, at concentrations ranging from 5 to 20 mg/mL, was investigated. Concentrations lower than 10 mg/mL have no cytotoxicity cultures of fibroblasts over 72 h. Further on, FSP membranes (FSP-M) were produced by spin coating to evaluate its properties. FSP-M shown having uniform surface as analyzed by Scanning Electron Microscopy (SEM). The relative amount of α-helix structures is higher when compared with the FSP-E. The FSP-M have higher temperature stability than the FSP-E, since they presented a denaturation temperature of 58.88 ± 3.36° C, according to the DSC analysis. FSP-M shown distinctive mechanical properties, with a stiffness of 16.57 ± 3.95 MPa and a yield strength of 23.85 ± 5.97 MPa. Human lung fibroblasts cell lines (MRC-5) were cultured in direct contact with FSP-M, demonstrating its cytocompatibility for 48 h. Based on these results, FSP can be considered a potential biomaterial recovered from nature, for wound dressing applications.This work was supported by the financial support from the Portuguese Foundation for Science and Technology (FCT) for the SV and SA PhD fellowship (PD/BD/135246/2017, SFRH/BD/112075/2015), ARF and EMF Post-Doctoral fellowships (SFRH/BPD/100760/2014, SFRH/BPD/96197/2013), Investigator Starting Grant of AM (IF/00376/2014), PATH (NORTE-08-5369-FSE-000037), SPARTAN (PTDC/CTM-BIO/4388/2014), 3BsCOP (PTDC/BBB-ECT/3213/2014 − (POCI-01-0145-FEDER-016712)) and FROnTHERA (NORTE-01-0145-FEDER-0000232).info:eu-repo/semantics/publishedVersionElsevierUniversidade do MinhoVieira, S. F.Franco, A. R.Fernandes, E. M.Amorim, S.Ferreira, H.Pires, R. A.Reis, R. L.Martins, A.Neves, N. M.2018-072018-07-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/56290engVieira S. F., Franco A. R., Fernandes E. M., Amorim S., Ferreira H., Pires R. A., Reis R. L., Martins A., Neves N. M. Fish sarcoplasmic proteins as a high value marine material for wound dressing applications, Colloids and Surfaces B: Biointerfaces, Vol. 167, pp. 310-317, doi:10.1016/j.colsurfb.2018.04.002, 20180927-776510.1016/j.colsurfb.2018.04.00229679807https://www.sciencedirect.com/science/article/pii/S0927776518302066info: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:RCAAP2023-07-21T12:48:05Zoai:repositorium.sdum.uminho.pt:1822/56290Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:46:15.589812Repositório 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 |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications |
title |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications |
spellingShingle |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications Vieira, S. F. Cytocompatibility membranes Physico-chemical characterization Sarcoplasmic proteins Spin coating Science & Technology |
title_short |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications |
title_full |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications |
title_fullStr |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications |
title_full_unstemmed |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications |
title_sort |
Fish sarcoplasmic proteins as a high value marine material for wound dressing applications |
author |
Vieira, S. F. |
author_facet |
Vieira, S. F. Franco, A. R. Fernandes, E. M. Amorim, S. Ferreira, H. Pires, R. A. Reis, R. L. Martins, A. Neves, N. M. |
author_role |
author |
author2 |
Franco, A. R. Fernandes, E. M. Amorim, S. Ferreira, H. Pires, R. A. Reis, R. L. Martins, A. Neves, N. M. |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Vieira, S. F. Franco, A. R. Fernandes, E. M. Amorim, S. Ferreira, H. Pires, R. A. Reis, R. L. Martins, A. Neves, N. M. |
dc.subject.por.fl_str_mv |
Cytocompatibility membranes Physico-chemical characterization Sarcoplasmic proteins Spin coating Science & Technology |
topic |
Cytocompatibility membranes Physico-chemical characterization Sarcoplasmic proteins Spin coating Science & Technology |
description |
Fish sarcoplasmic proteins (FSP) constitute around 25–30% of the total fish muscle protein. As the FSP are water soluble, FSP were isolated from fresh cod (Gadus morhua) by centrifugation. By SDS-PAGE, it was possible to determine the composition of FSP extracts (FSP-E). The FSP-E undergo denaturation at 44.12 ± 2.34° C, as characterized by differential scanning calorimetry thermograms (DSC). The secondary structure of FSP-E is mainly composed by α-helix structure, as determined by circular dichroism. The cytocompatibility of FSP-E, at concentrations ranging from 5 to 20 mg/mL, was investigated. Concentrations lower than 10 mg/mL have no cytotoxicity cultures of fibroblasts over 72 h. Further on, FSP membranes (FSP-M) were produced by spin coating to evaluate its properties. FSP-M shown having uniform surface as analyzed by Scanning Electron Microscopy (SEM). The relative amount of α-helix structures is higher when compared with the FSP-E. The FSP-M have higher temperature stability than the FSP-E, since they presented a denaturation temperature of 58.88 ± 3.36° C, according to the DSC analysis. FSP-M shown distinctive mechanical properties, with a stiffness of 16.57 ± 3.95 MPa and a yield strength of 23.85 ± 5.97 MPa. Human lung fibroblasts cell lines (MRC-5) were cultured in direct contact with FSP-M, demonstrating its cytocompatibility for 48 h. Based on these results, FSP can be considered a potential biomaterial recovered from nature, for wound dressing applications. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-07 2018-07-01T00:00:00Z |
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/1822/56290 |
url |
http://hdl.handle.net/1822/56290 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Vieira S. F., Franco A. R., Fernandes E. M., Amorim S., Ferreira H., Pires R. A., Reis R. L., Martins A., Neves N. M. Fish sarcoplasmic proteins as a high value marine material for wound dressing applications, Colloids and Surfaces B: Biointerfaces, Vol. 167, pp. 310-317, doi:10.1016/j.colsurfb.2018.04.002, 2018 0927-7765 10.1016/j.colsurfb.2018.04.002 29679807 https://www.sciencedirect.com/science/article/pii/S0927776518302066 |
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info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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