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Type: Artigo
Title: The role of dialysis and freezing on structural conformation, thermal properties and morphology of silk fibroin hydrogels
Author: Ribeiro, Marta
Moraes, Mariana A. de
Beppu, Marisa M.
Monteiro, Fernando J.
Ferraz, Maria P.
Abstract: Silk fibroin has been widely explored for many biomedical applications, due to its biocompatibility and biodegradability. The aim of this work was to study the role of dialysis and freezing on structural conformation, thermal properties and morphology of silk fibroin hydrogels. Hydrogels were prepared after 3 and 7 days of dialysis and the effect of freezing was analyzed. For that purpose, a part of the fibroin hydrogels underwent freezing at -20 °C for 24 h, followed by lyophilization and the rest of the hydrogels were kept at 8 °C for 24 h, with further lyophilization. The fibroin hydrogels were characterized by X-ray diffraction (XRD), Fourier transformed infrared spectroscopy (FTIR), thermogravimetric analysis (TGA) and scanning electron microscopy (SEM). Measurements by XRD and FTIR indicated that silk I and silk II structures were present in the fibroin hydrogels and that the secondary structure of fibroin is transformed mostly to β-sheet during the gelation process. Thermal analysis indicated that fibroin hydrogels are thermally stable with the degradation peak at around 330-340 °C. SEM micrographs showed porous structures and the fibroin hydrogels subjected to freezing presented a much larger pore size. Results indicate that the dialysis time and freezing did not alter the material crystallinity, conformation or thermal behavior; however, hydrogel microstructure was strongly affected by dialysis time and freezing, showing controlled pores size. This study provides fundamental knowledge on silk fibroin hydrogels preparation and properties and the studied hydrogels are promising to be used in the biomaterial field
Subject: Biomateriais
Country: Estados Unidos
Editor: Taylor & Francis
Rights: Fechado
Identifier DOI: 10.4161/biom.28536
Date Issue: 2014
Appears in Collections:FEQ - Artigos e Outros Documentos

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