Abstract
Collagen-based materials are widely used as adhesives in medicine and cosmetology. However, for several applications, their properties require modification. In this work, the influence of Melissa officinalis on the properties of collagen films was studied. Collagen was extracted from Silver Carp skin. 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. Antioxidant activity was determined by spectrophotometric methods using DPPH free radicals, FRAP, and CUPRAC methods. Total phenolic compounds were determined by the Folin–Ciocalteau method. It was found that the addition of Melissa officinalis modified the roughness of collagen films and their mechanical properties. Moreover, the obtained material has antioxidant properties. The parameters mentioned above are very important in potential applications of collagen films containing Melissa officinalis in cosmetics.
Highlights
Collagen comprises one of the most appropriable biomaterials due to its eminent biocompatibility, biodegradability, natural origin, and non-genicity
For amide I and amide II bands we did not observe the shift. This fact may suggest that the secondary structure of collagen type I was not changed after the addition of melissa to collagen solution
The performed infrared spectroscopy analysis confirmed the presence of collagen and indicated a band at 1377 cm−1, which represents O-H stretching in carboxylic acid and O-H band phenol group present in rosmaric, gallic, and phenolic acid in the Melissa officinalis extract
Summary
Collagen comprises one of the most appropriable biomaterials due to its eminent biocompatibility, biodegradability, natural origin, and non-genicity. It is used in medical applications such as drug delivery systems, material matrices, and scaffolds in tissue engineering [1,2,3,4,5]. The structure of collagen type I is described by three chains that form a triple-helical conformation. Each of the polypeptide chains creates hydroxyproline II type helix. It is firmed by amino acid content. The structure of modified collagen is both plant-dependent and type-of-extract-dependent, so it is necessary to research each plant extract and its influence on collagen properties separately
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