Self-assembling proteins can be used for higher performance, more sustainable skincare products

If you have a meticulous skincare routine, you know that personal skincare products (PSCPs) are a big business. The PSCP industry will reach $74.12 billion USD by 2027, with an annual growth rate of 8.64%. With such competition, companies are always looking to engineer themselves an edge, producing products that perform better without the downsides of current offerings.

In a new study published in ACS Applied Polymer Materials from the lab of Professor of Chemical and Biomolecular Engineering Jin Kim Montclare, researchers have created a novel protein-based gel as a potential ingredient in sustainable and high-performance PSCPs. This protein-based material, named Q5, could transform the rheological — or flow-related — properties of PSCPs, making them more stable under the slightly acidic conditions of human skin. This innovation could also streamline the creation of more eco-friendly skincare products, offering increased efficacy and durability while addressing market demands for ethically sourced ingredients.

Personal skincare products, ranging from beauty cosmetics to medical creams, rely on sophisticated “chassis” formulations — often emulsions or gels — to effectively deliver active ingredients. The performance of these products depends heavily on the stability and responsiveness of their chassis under various environmental conditions, particularly pH. 

Current formulations often rely on ingredients such as polysaccharides or synthetic polymers to achieve the desired texture, stability, and compatibility with skin's natural pH, which is mildly acidic (most human skin has a pH of between 5.4–5.9). However, these traditional rheological modifiers have raised environmental concerns regarding sourcing and sustainability.

To take on this challenge, Montclare and her colleagues fabricated a self-assembling coiled-coil protein they call Q5. In the study, Q5 demonstrated impressive pH stability. The protein's unique structure enables it to form strong gels that do not degrade easily under acidic conditions, enhancing the longevity and performance of skincare products.This resilience marks a significant improvement over earlier protein-based gels, which typically disassemble in lower pH environments.

Notably, the research suggests that Q5 could be produced sustainably via bacterial or yeast fermentation, circumventing the ethical and ecological issues associated with animal-derived proteins or synthetic polymers. The protein’s natural amphiphilicity — its ability to attract and retain moisture — also enables it to bind various molecules, adding versatility as a moisturizer or binding agent in skincare products.

The research suggests that these protein-based rheological modifiers like Q5 could soon become a valuable component in the next generation of high-performance skincare products, helping brands meet consumer demand for sustainable beauty solutions without compromising on quality or functionality.

About the New York University Tandon School of Engineering

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