review · International Journal of Pharmaceutics
Silk fibres produced by the Bombyx mori silkworm consist primarily of two proteins: hydrophobic silk fibroin, which provides structural strength, and hydrophilic silk sericin, which provides elasticity and binds the fibres together. Both proteins possess biocompatibility, biodegradability, and versatile structures that allow them to be engineered into diverse formats, including nanofibres, hydrogels, films, and micro-nanoparticles. Inherent functional groups allow these proteins to be chemically modified or cross-linked with other biomaterials, conferring antioxidant and antibacterial qualities to the resulting matrices. Due to these controllable physical, chemical, and biological features, these natural silk components are being explored for pharmaceutical and biomedical applications. These uses centre primarily on advanced platforms for tissue engineering, wound repair, and targeted drug delivery systems for cancer therapy.
Developing effective materials for wound management and cancer treatment requires substances that interact safely with the body and degrade naturally. Silkworm proteins offer renewable, tunable building blocks capable of carrying drugs or protecting wounded tissue while preventing bacterial growth. Translating these protein matrices into functional delivery systems and dressings could advance safer, more responsive therapeutic options.
These proteins could enable the development of advanced wound care dressings, tissue engineering scaffolds, and targeted oncology drug formulations for biomedical and pharmaceutical manufacturers. As this abstract describes a review of diverse formulation advancements rather than a specific evaluated prototype, the commercial readiness appears to be at the level of early-stage to applied laboratory research.
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Silks are a class of proteins generated naturally by different arthropods, including silkworms, spiders, scorpions, mites, wasps, and bees. This review discusses the silk fibroin and silk sericin fabricated by Bombyx mori silkworm as versatile fibers. This silk fiber is predominantly composed of hydrophobic silk fibroin and hydrophilic silk sericin. Fibroin is defined as a structural protein that bestows silk with strength, while sericin is characterized as a gum-like protein, tying the two fibrous proteins together and endowing silk proteins with elasticity. Due to their versatile structures, biocompatibility, and biodegradability, they could be tailored into intricate structures to warrant particular demands. The intrinsic functional groups of both proteins enable their functionalization and cross-linking with various biomaterials to endow the matrix with favorable antioxidant and antibacterial properties. Depending on the target applications, they can be integrated with other materials to formulate nanofibrous, hydrogels, films, and micro-nanoparticles. Given the outstanding biological and controllable physicochemical features of fibroin and sericin, they could be exploited in pharmaceutical applications involving tissue engineering, wound repair, drug delivery, and cancer therapy. This review comprehensively discusses the advancements in the implementation of different formulations of silk fibroin and sericin in wound healing and drug delivery systems, particularly for cancer treatment.
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DOI: 10.1016/j.ijpharm.2024.124494
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