This review provides a report on properties and recent advances in the application of collagen in cosmetics. Collagen is a structural protein found in animal organisms where it provides for the fundamental structural support. Most commonly it is extracted from mammalian and fish skin. Collagen has attracted significant academic interest as well as the attention of the cosmetic industry due to its interesting properties that include being a natural humectant and moisturizer for the skin. This review paper covers the biosynthesis of collagen, the sources of collagen used in the cosmetic industry, and the role played by this protein in cosmetics. Future aspects regarding applications of collagen-based materials in cosmetics have also been mentioned.

In this review, we provide a report on recent studies in the field of research on the blends of hyaluronic acid with other natural polymers, namely collagen and chitosan. Hyaluronic acid has attracted significant interest in biomedical and cosmetic applications due to its interesting properties. In recent years, blends of hyaluronic acid with other polymers have been studied for new materials development. New materials may show improved properties that are important in the biomedical applications and in cosmetic preparations. In this review paper, the structure, preparation, and properties of hyaluronic acid blends with collagen and chitosan have been discussed and examples of new materials based on such blends have been presented. A comparison of the currently available information in the field has been shown. Future aspects in the field of hyaluronic acid blends and their applications in the biomedical and cosmetic industry have also been mentioned.

The ability to form strong intermolecular interactions by linear glucosamine polysaccharides with collagen is strictly related to their nonlinear dynamic behavior and hence bio-lubricating features. Type III collagen plays a crucial role in tissue regeneration, and its presence in the articular cartilage affects its bio-technical features. In this study, the molecular dynamics methodology was applied to evaluate the effect of deacetylation degree on the chitosan affinity to type III collagen. The computational procedure employed docking and geometry optimizations of different chitosan structures characterized by randomly distributed deacetylated groups. The eight different degrees of deacetylation from 12.5% to 100% were taken into account. We found an increasing linear trend (R2 = 0.97) between deacetylation degree and the collagen–chitosan interaction energy. This can be explained by replacing weak hydrophobic contacts with more stable hydrogen bonds involving amino groups in N-deacetylated chitosan moieties. In this study, the properties of chitosan were compared with hyaluronic acid, which is a natural component of synovial fluid and cartilage. As we found, when the degree of deacetylation of chitosan was greater than 0.4, it exhibited a higher affinity for collagen than in the case of hyaluronic acid.

In this work, the interactions between hyaluronic acid and bovine serum albumin were investigated. The film-forming properties of the mixture were proven, and the mechanical and surface properties of the films were measured. The results showed the interactions between hyaluronic acid and albumin, mainly by hydrogen bonds. Molecular docking was used for the visualization of the interactions. The films obtained from the mixture of hyaluronic acid possessed different properties to films obtained from the single component. The addition of bovine serum albumin to hyaluronic acid led to a decrease in the mechanical properties, and to an increase in the surface roughness of the film. The new materials that have been obtained by blending can form a new group of materials for biomedicine and cosmetology.