Protein Assemblies & Aggregates I
2/3/2013 1:45:00 PM
ARTIFICIAL HONEYBEE SILK: A RECOMBINANT PROTEIN AS A BIOMIMETIC STRUCTURAL MATERIAL
Jeffrey S. Church
, Mickey G. Huson
, Tara D. Sutherland
CSIRO Materials Science and Engineering, Belmont, Australia,
CSIRO Ecosystem Sciences, Acton, Australia.
Honeybee larvae produce silken cocoons that provide mechanical stability to the hive. The silk proteins are small and non-repetitive and therefore can be produced at large scale by fermentation in
. Recombinant silk proteins which have a coiled coil structure can be fabricated into a range of forms including sponges and fibers. The resultant material is soluble in water and requires a post-production stabilizing treatment. Aqueous methanol treatment induces the formation of a stabilizing ß-sheet structure, with the amount of ß-sheet being controlled by time or methanol concentration. Dry heat treatment at 190°C also produces a water insoluble material but without significant secondary structural changes. Honeybee silk proteins are particularly high in lysine, serine, threonine, glutamic acid and aspartic acid. The stability of the heat treated material is attributed to the generation of covalent cross-links including lysinoalanine and isopeptide groups. The unique ability to stabilize material by controlling secondary structure rearrangement and covalent cross-linking allows us to design recombinant silk materials with a wide range of properties and potential applications.
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