Recombinant Production, Characterization, and Fiber Spinning of an Engineered Short Major Ampullate Spidroin (MaSp1s)

Spider dragline silk exhibits an extraordinary toughness and is typically composed of two types of major ampullate spidroins (MaSp1 and MaSp2), differing in their proline content and hydrophobicity. In this paper, we recombinantly produced an unusual but naturally occurring short major ampullate spidroin (MaSp1s) as a fusion construct between established Latrodectus hesperus terminal domains and the novel Cyrtophora moluccensis core domain. The sequence of the recombinant spidroin was engineered to guarantee high yields upon recombinant production and was named eMaSp1s. Its solution structure as well as the mechanical properties of wet-spun eMaSp1s fibers were examined. Structural characterization using CD- and FTIR spectroscopy showed a predominantly α-helical solution structure and a high ß-sheet content within fibers. Surprisingly, eMaSp1s fibers show similar mechanical properties as wet-spun fibers of other engineered spider silk proteins, albeit eMaSp1s has a lower molecular weight and not the typical sequence repeats in its core domain. Therefore, the findings provide insights into the molecular interplay necessary to obtain the typical silk fiber mechanics.