Genetically Engineered Spider Silk for Disulfide-Mediated Multimerisation and Covalent Coupling

摘要

Native spider silk shows fascinating mechanical properties, with high tensile strength and elasticity compared to other biopolymers in nature. These extreme properties, combined with its biocompatibility, make spider silk a highly interesting biomaterial for various medical and biotechnological applications. Spider silk is mainly composed of proteins with highly repetitive amino acid sequence (approximately 100 recurrent poly-alanine blocks interrupted by glycine-rich regions) and nonrepetitive N- and C-terminal domains. The C-terminal domain can form disulfide-mediated dimers and is important for fiber formation. Unfortunately, spider silk has proven to be difficult to produce recombinantly, mainly due to the highly repetitive sequences and poor protein solubility. However, our group has managed to clone and express a miniature spider silk protein, containing only four poly-