Hair perfumes are becoming a trend all over the world and new cosmetic formulations have been developed to address this recent need. In the present study, we developed a system for the controlled delivery of perfumes on hair, based on zein, a protein derived from maize, and on keratin. The Keratin:Zein particles, obtained using different strategies and proportions of zein and keratin, presented a high stability along storage, related with the presence of keratin on the particles' formulation. When applied on hair, the particles formed a film-like structure over the fibers. Fragrance diffusion from the hair-coated particles was dependent on the temperature, the method of particles' preparation and the fragrances' physicochemical properties (melting point and vapor pressure). The particles formulations showed also the capacity to improve hair's mechanical properties and hydration degree. The new system based on Keratin:Zein particles revealed high potential for the development of personalized hair cosmetic products allowing adjustments depending on the personal sensory preferences.
The perming of hair is a common styling procedure with negative impact on the overall properties of the hair fibers. Usually, this process uses harsh chemicals to promote the disruption of disulfide bonds and the formation of new bonds to change the shape of hair. Here, we explored bovine serum albumin (BSA), silk fibroin (SF), keratin and two fusion recombinant proteins (KP-UM and KP-Cryst) as new perming agents. A phosphate buffer prepared at different pH values (5, 7 and 9) was used to apply the proteins to virgin Asian hair, and a hot BaByliss was used to curl the hair fibers. To assess the potential of the protein formulations for hair styling, the perming efficiency and the perming resistance to wash were measured. Furthermore, the fiber water content was evaluated to assess if the proteins protected the hair during the styling process. Despite all of the proteins being able to assist in the curling of Asian hair, the best perming efficiency and perming resistance to wash results were observed for BSA and keratin. These proteins showed perming efficiency values close to that measured for a commercial perming product (chemical method), particularly at pH 5 and 9. The increase in the hair’s internal and external water contents revealed a protective effect provided by the proteins during the application of heat in the styling procedure. This study shows the potential of proteins to be used in the development of new eco-friendly hair styling products.
Onychomycosis is the most common nail fungal infection worldwide. There are several therapy options available for onychomycosis, such as oral antifungals, topicals, and physical treatments. Terbinafine is in the frontline for the treatment of onychomycosis; however, several adverse effects are associated to its oral administration. In this work, innovative keratin-based carriers encapsulating terbinafine were designed to overcome the drawbacks related to the use this drug. Therapeutic textiles functionalized with keratin-based particles (100% keratin; 80% keratin/20% keratin-PEG) encapsulating terbinafine were developed. The controlled release of terbinafine from the functionalized textiles was evaluated against different mimetic biologic solutions (PBS buffer—pH = 7.4, micellar solution and acidic sweat solution—pH = 4.3). The modification of keratin with polyethylene glycol (PEG) moieties favored the release of terbinafine at the end of 48 h for all the solution conditions. When the activity of functionalized textiles was tested against Trichophyton rubrum, a differentiated inhibition was observed. Textiles functionalized with 80% keratin/20% keratin-PEG encapsulating terbinafine showed a 2-fold inhibition halo compared with the textiles containing 100% keratin-encapsulating terbinafine. No activity was observed for the textiles functionalized with keratin-based particles without terbinafine. The systems herein developed revealed therapeutic potential towards nail fungal infections, taking advantage of keratin-based particles affinity to keratin structures and of the keratinase activity of T. rubrum.
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