Recombinant production of self-assembling proteins

Recombinant production of self-assembling proteins 4.2.1. Silks 

Cappello et al. (1990) pioneered the genetic engineering of repetitive building blocks. Working with the silkworm fibroin, they found that by starting with short oligonucleotide repeats, the size of the protein generated 

Yeast and bacterial systems often give low levels of expression of silks, and this has led to the development of production systems in tobacco and potato. Scheller et al. (2001) have shown that spider silk proteins can be produced in transgenic plants. They inserted synthetic spider silk protein (spidroin) genes into transgenic plants under the control of the CaMV35S promoter. Using this system they were able to demonstrate the accumulation of recombinant silk proteins to a level of at least 2% of total soluble protein in the endoplasmic reticulum of tobacco leaves, and potato tubers. 

There are several reports of the use of silk in biomaterials. Kluge et al. (2008) provide a good overview of application of spider silks including recombinant versions. In addition to spider silks there are other types of silks that provide distinct and useful properties, such as those derived from mussels which will presumably become targets for recombinant protein production (Carrington, 2008). 

Girotti et al. (2004) have designed and bio-produced elastin-like protein polymers (ELP) which contain biofunctional motifs with cell adhesion sequences required for tissue-engineering applications. The protein polymer contained periodically spaced fibronectin CS5 domains enclosing the cell attachment sequence REDV. The overall sequence, 

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See also in sourсe #XX -- [ , , ]

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