Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/51439 http://dx.doi.org/10.3390/molecules22081368 |
Resumo: | Miscibility is an important issue in biopolymer blends for analysis of the behavior of polymer pairs through the detection of phase separation and improvement of the mechanical and physical properties of the blend. This study presents the formulation of a stable and one-phase mixture of collagen and regenerated silk fibroin (RSF), with the highest miscibility ratio between these two macromolecules, through inducing electrostatic interactions, using salt ions. For this aim, a ternary phase diagram was experimentally built for the mixtures, based on observations of phase behavior of blend solutions with various ratios. The miscibility behavior of the blend solutions in the miscible zones of the phase diagram was confirmed quantitatively by viscosimetric measurements. Assessing the effects of biopolymer mixing ratio and salt ions, before and after dialysis of blend solutions, revealed the importance of ion-specific interactions in the formation of coacervate-based materials containing collagen and RSF blends that can be used in pharmaceutical, drug delivery, and biomedical applications. Moreover, the conformational change of silk fibroin from random coil to beta sheet, in solution and in the final solid films, was detected by circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR), respectively. Scanning electron microscopy (SEM) exhibited alterations of surface morphology for the biocomposite films with different ratios. Surface contact angle measurement illustrated different hydrophobic properties for the blended film surfaces. Differential scanning calorimetry (DSC) showed that the formation of the beta sheet structure of silk fibroin enhances the thermal stability of the final blend films. Therefore, the novel method presented in this study resulted in the formation of biocomposite films whose physico-chemical properties can be tuned by silk fibroin conformational changes by applying different component mixing ratios. |
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Ghaeli, Imade Moraes, Mariana A. [UNIFESP]Beppu, Marisa M.Lewandowska, KatarzynaSionkowska, AlinaFerreira-da-Silva, FredericoFerraz, Maria P.Monteiro, Fernando J.2019-08-19T11:49:56Z2019-08-19T11:49:56Z2017Molecules. Basel, v. 22, n. 8, p. -, 2017.1420-3049http://repositorio.unifesp.br/handle/11600/51439http://dx.doi.org/10.3390/molecules22081368WOS000408602900131.pdf10.3390/molecules22081368WOS:000408602900131Miscibility is an important issue in biopolymer blends for analysis of the behavior of polymer pairs through the detection of phase separation and improvement of the mechanical and physical properties of the blend. This study presents the formulation of a stable and one-phase mixture of collagen and regenerated silk fibroin (RSF), with the highest miscibility ratio between these two macromolecules, through inducing electrostatic interactions, using salt ions. For this aim, a ternary phase diagram was experimentally built for the mixtures, based on observations of phase behavior of blend solutions with various ratios. The miscibility behavior of the blend solutions in the miscible zones of the phase diagram was confirmed quantitatively by viscosimetric measurements. Assessing the effects of biopolymer mixing ratio and salt ions, before and after dialysis of blend solutions, revealed the importance of ion-specific interactions in the formation of coacervate-based materials containing collagen and RSF blends that can be used in pharmaceutical, drug delivery, and biomedical applications. Moreover, the conformational change of silk fibroin from random coil to beta sheet, in solution and in the final solid films, was detected by circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR), respectively. Scanning electron microscopy (SEM) exhibited alterations of surface morphology for the biocomposite films with different ratios. Surface contact angle measurement illustrated different hydrophobic properties for the blended film surfaces. Differential scanning calorimetry (DSC) showed that the formation of the beta sheet structure of silk fibroin enhances the thermal stability of the final blend films. Therefore, the novel method presented in this study resulted in the formation of biocomposite films whose physico-chemical properties can be tuned by silk fibroin conformational changes by applying different component mixing ratios.FEDER funds through the Programa Operacional Factores de Competitividade (COMPETE)Portuguese funds through FCT (Fundação para a Ciencia e a Tecnologia)European Cooperation in Science and Technology (COST)Univ Porto, i3S, Rua Alfredo Allen 208, P-4200135 Oporto, PortugalUniv Porto, INEB Inst Engn Biomed, Rua Alfredo Allen 208, P-4200135 Oporto, PortugalUniv Porto, Dept Engn Met & Mat, FEUP, Fac Engn, P-4200465 Oporto, PortugalUniv Estadual Campinas, Sch Chem Engn, BR-13083852 Campinas, SP, BrazilUniv Fed São Paulo, Dept Chem Engn, BR-09913030 Diadema, BrazilNicolaus Copernicus Univ Torun, Dept Chem Biomat & Cosmet, Fac Chem, Ul Gagarina 7, PL-87100 Torun, PolandUniv Porto, IBMC, Rua Alfredo Allen 208, P-4200135 Oporto, PortugalUniv Fernando Pessoa, Energy Environm & Hlth Res Unit, FP ENAS CEBIMED, Biomed Res Ctr, P-200150 Oporto, PortugalUniv Fed São Paulo, Dept Chem Engn, BR-09913030 Diadema, BrazilFEDER: POCI/01/0145/FEDER/007265FCT: PT2020 UID/QUI/50006/2013European Cooperation in Science and Technology (COST): Action MP1301Web of Science-engMdpibiopolymersprotein-protein interactionsilk fibroinmiscibilitycoacervationPhase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid Stateinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000408602900131.pdfapplication/pdf6492493${dspace.ui.url}/bitstream/11600/51439/1/WOS000408602900131.pdf6f23e1cf4f7f7a7f9067183eaa16ecd4MD51open accessTEXTWOS000408602900131.pdf.txtWOS000408602900131.pdf.txtExtracted texttext/plain72173${dspace.ui.url}/bitstream/11600/51439/8/WOS000408602900131.pdf.txt176a83e3ba11275f8c04681a5dbe27deMD58open accessTHUMBNAILWOS000408602900131.pdf.jpgWOS000408602900131.pdf.jpgIM Thumbnailimage/jpeg6790${dspace.ui.url}/bitstream/11600/51439/10/WOS000408602900131.pdf.jpgc7e77656cf72484de07a0c345700eb0eMD510open access11600/514392023-06-05 19:32:09.007open accessoai:repositorio.unifesp.br:11600/51439Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-06-05T22:32:09Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State |
title |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State |
spellingShingle |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State Ghaeli, Ima biopolymers protein-protein interaction silk fibroin miscibility coacervation |
title_short |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State |
title_full |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State |
title_fullStr |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State |
title_full_unstemmed |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State |
title_sort |
Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State |
author |
Ghaeli, Ima |
author_facet |
Ghaeli, Ima de Moraes, Mariana A. [UNIFESP] Beppu, Marisa M. Lewandowska, Katarzyna Sionkowska, Alina Ferreira-da-Silva, Frederico Ferraz, Maria P. Monteiro, Fernando J. |
author_role |
author |
author2 |
de Moraes, Mariana A. [UNIFESP] Beppu, Marisa M. Lewandowska, Katarzyna Sionkowska, Alina Ferreira-da-Silva, Frederico Ferraz, Maria P. Monteiro, Fernando J. |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Ghaeli, Ima de Moraes, Mariana A. [UNIFESP] Beppu, Marisa M. Lewandowska, Katarzyna Sionkowska, Alina Ferreira-da-Silva, Frederico Ferraz, Maria P. Monteiro, Fernando J. |
dc.subject.eng.fl_str_mv |
biopolymers protein-protein interaction silk fibroin miscibility coacervation |
topic |
biopolymers protein-protein interaction silk fibroin miscibility coacervation |
description |
Miscibility is an important issue in biopolymer blends for analysis of the behavior of polymer pairs through the detection of phase separation and improvement of the mechanical and physical properties of the blend. This study presents the formulation of a stable and one-phase mixture of collagen and regenerated silk fibroin (RSF), with the highest miscibility ratio between these two macromolecules, through inducing electrostatic interactions, using salt ions. For this aim, a ternary phase diagram was experimentally built for the mixtures, based on observations of phase behavior of blend solutions with various ratios. The miscibility behavior of the blend solutions in the miscible zones of the phase diagram was confirmed quantitatively by viscosimetric measurements. Assessing the effects of biopolymer mixing ratio and salt ions, before and after dialysis of blend solutions, revealed the importance of ion-specific interactions in the formation of coacervate-based materials containing collagen and RSF blends that can be used in pharmaceutical, drug delivery, and biomedical applications. Moreover, the conformational change of silk fibroin from random coil to beta sheet, in solution and in the final solid films, was detected by circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR), respectively. Scanning electron microscopy (SEM) exhibited alterations of surface morphology for the biocomposite films with different ratios. Surface contact angle measurement illustrated different hydrophobic properties for the blended film surfaces. Differential scanning calorimetry (DSC) showed that the formation of the beta sheet structure of silk fibroin enhances the thermal stability of the final blend films. Therefore, the novel method presented in this study resulted in the formation of biocomposite films whose physico-chemical properties can be tuned by silk fibroin conformational changes by applying different component mixing ratios. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017 |
dc.date.accessioned.fl_str_mv |
2019-08-19T11:49:56Z |
dc.date.available.fl_str_mv |
2019-08-19T11:49:56Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
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article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Molecules. Basel, v. 22, n. 8, p. -, 2017. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/51439 http://dx.doi.org/10.3390/molecules22081368 |
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1420-3049 |
dc.identifier.file.none.fl_str_mv |
WOS000408602900131.pdf |
dc.identifier.doi.none.fl_str_mv |
10.3390/molecules22081368 |
dc.identifier.wos.none.fl_str_mv |
WOS:000408602900131 |
identifier_str_mv |
Molecules. Basel, v. 22, n. 8, p. -, 2017. 1420-3049 WOS000408602900131.pdf 10.3390/molecules22081368 WOS:000408602900131 |
url |
http://repositorio.unifesp.br/handle/11600/51439 http://dx.doi.org/10.3390/molecules22081368 |
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eng |
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