Major ampullate (MA) spider silk has fascinating mechanical properties combining strength and elasticity. All known natural MA silks contain at least two or more different spidroins; however, it is unknown why and if there is any interplay in the spinning dope. Here, two different spidroins from Araneus diadematus are co-produced in Escherichia coli to study the possible dimerization and effects thereof on the mechanical properties of fibers. During the production of the two spidroins, a mixture of homo- and heterodimers is formed triggered by the carboxyl-terminal domains. Interestingly, homodimeric species of the individual spidroins self-assemble differently in comparison to heterodimers, and stoichiometric mixtures of homo- and heterodimers yield spidroin networks upon assembly with huge impact on fiber mechanics upon spinning. The obtained results provide the basis for man-made tuning of spinning dopes to yield high-performance fibers.
Keywords: bioinspired fibers; heterodimers; protein interplay; self-assembly; spider silk.
© 2021 The Authors. Advanced Materials published by Wiley-VCH GmbH.