Abstract
Collagen possesses unique properties, e.g., biocompatibility, biodegradability, and non-toxicity. However, collagen material degrades too quickly and has low mechanical properties. One of the methods of polymers’ modification is mixing them to obtain blends. In this study, the influence of β-glucan for collagen material was analyzed. The interaction between the functional groups of the polymer was analyzed by ATR-FTIR (attenuated total reflection-fourier transform infrared) spectroscopy. The influence of β-glucan on mechanical properties was evaluated. The surface properties of materials were assessed using contact angle measurements and the topography of materials was evaluated by AFM (atomic force microscope). The structure of materials was analyzed according to SEM (scanning electron microscopy) pictures. Moreover, the DPPH-free radicals’ scavenging ability and biocompatibility against erythrocytes and HaCaT cells were evaluated. Collagen and β-glucan were bound together by a hydrogen bond. β-glucan addition increased the roughness of the surface of the film and resulted in a more rigid character of the materials. A small addition of β-glucan to collagen provided a more hydrophilic character. All the materials could swell in in vitro conditions and showed antioxidant activity. Materials do not cause erythrocyte hemolysis. Finely, our cytotoxicity studies indicated that β-glucan can be safely added at small (10% or less) quantity to collagen matrix, they sufficiently support cell growth, and the degradation products of such matrices may actually provide some beneficial effects to the surrounding cells/tissues.
Highlights
Introduction published maps and institutional affilCollagens are a group of major structural proteins
Hydrogen bonds between collagen and β-glucan are formed by inter3.1
Collagen from fish can be mixed with β-glucan and prepared in the form of thin films by using the solvent casting method
Summary
Introduction published maps and institutional affilCollagens are a group of major structural proteins. The main sources of collagen for industrial applications are bovine and pig’s skins and bones [3]. Their application has been restricted due to the outbreak of some diseases, such as foot and mouth disease (FMD) and bovine spongiform encephalopathy (BSE), which may be transferred to humans [4]. Those sources of collagen are not acceptable in research by some cultures [5].
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