![]() These micelles subsequently aggregated into larger 'globules' and gel-like states as the concentration of silk fibroin increased, while maintaining solubility owing to the hydrophilic regions of the protein interspersed among the larger hydrophobic regions. The sizes (100-200 nm diameter) of these structures could be predicted from hydrophobicity plots of silk protein primary sequence. Here we report the identification of emulsion formation and micellar structures from aqueous solutions of reconstituted silkworm silk fibroin as a first step in the process to control water and protein-protein interactions. The lack of understanding of the protein processing in silk glands has prevented the recapitulation of these properties in vitro from reconstituted or genetically engineered silks. Silk scaffolds have been successfully used in wound healing and in tissue engineering of bone, cartilage, tendon and ligament tissues.Ībstract: Silk spinning by insects and spiders leads to the formation of fibres that exhibit high strength and toughness. Silk biomaterials are biocompatible when studied in vitro and in vivo. Several primary cells and cell lines have been successfully grown on different silk biomaterials to demonstrate a range of biological outcomes. The degradability of silk biomaterials can be related to the mode of processing and the corresponding content of β-sheet crystallinity. Molecular engineering of silk sequences has been used to modify silks with specific features, such as cell recognition or mineralization. Silks can be chemically modified through amino acid side chains to alter surface properties or to immobilize cellular growth factors. Recently regenerated silk solutions have been used to form a variety of biomaterials, such as gels, sponges and films, for medical applications. Silk fibers in the form of sutures have been used for centuries. With the diversity of silk-like fibrous proteins from spiders and insects, a range of native or bioengineered variants can be expected for application to a diverse set of clinical needs.Ībstract: Silks are fibrous proteins with remarkable mechanical properties produced in fiber form by silkworms and spiders. To date, studies with silks to address biomaterial and matrix scaffold needs have focused on silkworm silk. For example, in designing scaffolds for tissue engineering these properties are particularly relevant and recent results with bone and ligament formation in vitro support the potential role for this biomaterial in future applications. Furthermore, the unique mechanical properties of the silk fibers, the diversity of side chain chemistries for ‘decoration’ with growth and adhesion factors, and the ability to genetically tailor the protein provide additional rationale for the exploration of this family of fibrous proteins for biomaterial applications. ![]() More recent studies with well-defined silkworm silk fibers and films suggest that the core silk fibroin fibers exhibit comparable biocompatibility in vitro and in vivo with other commonly used biomaterials such as polylactic acid and collagen. During the past 20 years, some biocompatibility problems have been reported for silkworm silk however, contamination from residual sericin (glue-like proteins) was the likely cause. The unique mechanical properties of these fibers provided important clinical repair options for many applications. ![]() Abstract: Silk from the silkworm, Bombyx mori, has been used as biomedical suture material for centuries.
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