Structural Characterization of a Directed Self-Assembly Recombinant Quasi-Spider Silk Protein Expressed in Escherichia coli

Native spider silk protein is an extracellular fibrous protein with distinctive characteristics of elasticity and strength. However, its application was limited for several shortcomings. Here we expressed a recombinant quasi-spider silk protein in which collagen-like peptides were fused to the spider silk protein in Escherichia coli. This recombinant protein is a "ABA" type triblock copolymer. Part A which located in both ends of the protein composed of (Pro-Gly-Pro)(n) homopolymeric stretches, formed the orientable collagen three-helix structure. While, the intervening block (part B) is the spider silk protein which is optimally designed. Results showed that the interest protein gene was successfully expressed in Escherichia coli. Structure characterization of this recombinant protein indicates tremendous potential usage in new biomedical material field. (C) 2019 Friends Science Publishers