Abstract
Collagen films are widely used as adhesives in medicine and cosmetology. However, its properties require modification. In this work, the influence of salicin on the properties of collagen solution and films was studied. Collagen was extracted from silver carp skin. The rheological properties of collagen solutions with and without salicin were characterized by steady shear tests. Thin collagen films were prepared by solvent evaporation. The structure of films was researched using infrared spectroscopy. The surface properties of films were investigated using Atomic Force Microscopy (AFM). Mechanical properties were measured as well. It was found that the addition of salicin modified the roughness of collagen films and their mechanical and rheological properties. The above-mentioned parameters are very important in potential applications of collagen films containing salicin.
Highlights
Rheological and Film-FormingCollagen-based biomaterials are widely used in the pharmacological, medical, and cosmetological fields due to their biocompatibility, non-toxicity, and natural origin [1,2,3].Collagen type I which is widely applied in the above-mentioned fields is composed of three polypeptide chains coiled around each other
The results showed that the addition of salicin to the collagen solutions increases the apparent viscosity of a solution
Willow bark extract containing salicin can be incorporated into collagen solutions and films
Summary
Collagen type I which is widely applied in the above-mentioned fields is composed of three polypeptide chains coiled around each other. The molecule is held together mainly by hydrogen bindings among groups such as CO and NH. The maintenance of this protein structure in its mature form is ensured by covalent bonds [4,5]. Triple helices are being arranged to flexible fibrils that can be further cross-linked to improve the mechanical resistance of the collagen material [6,7]. Individual triple-helical domain pertains further than 95% of the molecule in the classic fibril-forming collagens. In some of the collagens, it occurs that the triple-helical domain constitutes only a fraction of the molecule’s mass, but the triple-helices are multiple [8,9,10,11,12]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
