Publications by authors named "Kelvin O Moseti"

Silk fibroin (SF) has attracted attention as a base biomaterial that could be suitable in many applications because of its shape and structure. Highly functional SF has been developed to promote tissue regeneration with heparin conjugation. However, the hydrophobic three-dimensional structure of SF makes it difficult to bind to high-molecular-weight and hydrophilic compounds such as heparin.

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Silk fibroin (SF) produced by the domesticated wild silkworm, () is attracting increasing interest owing to its unique mechanical properties, biocompatibility, and abundance in nature. However, its utilization is limited, largely due to lack of appropriate processing strategies. Various strategies have been assessed to regenerate cocoon SF, as well as the use of aqueous liquid fibroin (LF) prepared by dissolution of silk dope obtained from the silk glands of mature silkworm larvae in water.

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Formation of the -helical conformation in the poly-l-alanine (PA) sequence regions, subsequent structural transition to -sheet during natural spinning, and presence of residual -helices in () native silk fiber have been experimentally proven. However, the aggregation state of the residual -helices, and their influence on the mechanical deformation behavior in native fiber remain unclear. Here we show that the -helices form an ordered aggregation state with a hexagonal packing in the aqueous solution, some of which remain during natural spinning.

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