Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State

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dc.contributor.authorGhaeli, Ima
dc.contributor.authorde Moraes, Mariana A. [UNIFESP]
dc.contributor.authorBeppu, Marisa M.
dc.contributor.authorLewandowska, Katarzyna
dc.contributor.authorSionkowska, Alina
dc.contributor.authorFerreira-da-Silva, Frederico
dc.contributor.authorFerraz, Maria P.
dc.contributor.authorMonteiro, Fernando J.
dc.date.accessioned2019-08-19T11:49:56Z
dc.date.available2019-08-19T11:49:56Z
dc.date.issued2017
dc.description.abstractMiscibility 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.en
dc.description.affiliationUniv Porto, i3S, Rua Alfredo Allen 208, P-4200135 Oporto, Portugal
dc.description.affiliationUniv Porto, INEB Inst Engn Biomed, Rua Alfredo Allen 208, P-4200135 Oporto, Portugal
dc.description.affiliationUniv Porto, Dept Engn Met & Mat, FEUP, Fac Engn, P-4200465 Oporto, Portugal
dc.description.affiliationUniv Estadual Campinas, Sch Chem Engn, BR-13083852 Campinas, SP, Brazil
dc.description.affiliationUniv Fed São Paulo, Dept Chem Engn, BR-09913030 Diadema, Brazil
dc.description.affiliationNicolaus Copernicus Univ Torun, Dept Chem Biomat & Cosmet, Fac Chem, Ul Gagarina 7, PL-87100 Torun, Poland
dc.description.affiliationUniv Porto, IBMC, Rua Alfredo Allen 208, P-4200135 Oporto, Portugal
dc.description.affiliationUniv Fernando Pessoa, Energy Environm & Hlth Res Unit, FP ENAS CEBIMED, Biomed Res Ctr, P-200150 Oporto, Portugal
dc.description.affiliationUnifespUniv Fed São Paulo, Dept Chem Engn, BR-09913030 Diadema, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFEDER funds through the Programa Operacional Factores de Competitividade (COMPETE)
dc.description.sponsorshipPortuguese funds through FCT (Fundação para a Ciencia e a Tecnologia)
dc.description.sponsorshipEuropean Cooperation in Science and Technology (COST)
dc.description.sponsorshipIDFEDER: POCI/01/0145/FEDER/007265
dc.description.sponsorshipIDFCT: PT2020 UID/QUI/50006/2013
dc.description.sponsorshipIDEuropean Cooperation in Science and Technology (COST): Action MP1301
dc.format.extent-
dc.identifierhttp://dx.doi.org/10.3390/molecules22081368
dc.identifier.citationMolecules. Basel, v. 22, n. 8, p. -, 2017.
dc.identifier.doi10.3390/molecules22081368
dc.identifier.fileWOS000408602900131.pdf
dc.identifier.issn1420-3049
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/51439
dc.identifier.wosWOS:000408602900131
dc.language.isoeng
dc.publisherMdpi
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectbiopolymersen
dc.subjectprotein-protein interactionen
dc.subjectsilk fibroinen
dc.subjectmiscibilityen
dc.subjectcoacervationen
dc.titlePhase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid Stateen
dc.typeinfo:eu-repo/semantics/article
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