Silk from the silkworm, Bombyx mori,has been used as biomedical suture material for centuries. The unique mechanical
properties of these fibers provided important clinical repair options for many applications. 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. 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. 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. 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. To date,studies with silks to address biomaterial and matrix scaffold needs have focused on
silkworm silk. 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.
Silk from the silkworm, Bombyx mori,has been used as biomedical suture material for centuries. The unique mechanical
properties of these fibers provided important clinical repair options for many applications. 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. 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. 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. 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. To date,studies with silks to address biomaterial and matrix scaffold needs have focused on
silkworm silk. 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.
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