【Frontiers in HaiChuan Chemical Technology】New progress has been made in protein protection research at East China University of Science and Technology; it has been discovered that inexpensive sericin protein has the ability to stabilize proteins

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Recently, the research group led by Professor Liu Runhui from the School of Materials Science and Engineering at East China University of Science and Technology reported the use of sericin, a natural resource waste from the silk industry, to achieve excellent stabilizing effects for proteins under various environmental stresses, providing comprehensive protection that cannot be achieved by a single protective agent. This achievement was published in CCS Chemistry, the flagship journal of the Chinese Chemical Society. 　　It is known that proteins are widely used as therapeutic agents and biocatalysts for treating various serious diseases as well as in industrial production. However, the inherent instability of proteins makes them susceptible to various environmental stresses during production, manufacturing, storage, transportation, and application, leading to conformational changes that severely impair their stability and efficacy and limit their use. Therefore, helping proteins maintain their conformation, preventing protein aggregation, and promoting the refolding of proteins under environmental stress are crucial for preserving their biological activity. 　　Inspired by LEA proteins, a class of special molecular chaperones with high hydrophilicity and no defined structure that are abundant in late embryogenesis, the research team focused on sericin, a natural protein derived from the outer layer of silk – a natural protein with high hydrophilicity and a high content of random coils. The research team found that sericin possesses chaperone-like activity, enabling it to effectively stabilize proteins with various physicochemical properties under various environmental stresses (including high temperatures, mechanical forces, acidic conditions, the presence of organic solvents, freeze-drying, and repeated freezing-thawing), something that is difficult to achieve with commonly used single protectants. Mechanistic studies have shown that sericin protects proteins from environmental stresses by forming a barrier through protein-protein interactions. It is worth noting that as a by-product of the silk industry, sericin is not only easily available and inexpensive, but also possesses excellent biocompatibility. This gives it unique practical value and broad application prospects in areas such as the preservation of protein-based drugs, the development of biological agents, and the use of industrial enzymes.