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

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

Author Ghaeli, Ima Google Scholar
de Moraes, Mariana A. Autor UNIFESP Google Scholar
Beppu, Marisa M. Google Scholar
Lewandowska, Katarzyna Google Scholar
Sionkowska, Alina Google Scholar
Ferreira-da-Silva, Frederico Google Scholar
Ferraz, Maria P. Google Scholar
Monteiro, Fernando J. Google Scholar
Abstract 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.
Keywords biopolymers
protein-protein interaction
silk fibroin
Language English
Sponsor 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)
Grant number FEDER: POCI/01/0145/FEDER/007265
FCT: PT2020 UID/QUI/50006/2013
European Cooperation in Science and Technology (COST): Action MP1301
Date 2017
Published in Molecules. Basel, v. 22, n. 8, p. -, 2017.
ISSN 1420-3049 (Sherpa/Romeo, impact factor)
Publisher Mdpi
Extent -
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000408602900131

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