Biomacromolecules, Vol.18, No.1, 231-241, 2017
Nanoscale Structural Features in Major Ampullate Spider Silk
Spider major ampullate silk is often schematically represented as a two-phase material composed of crystalline nanodomains in an amorphous matrix. Here we are interested in revealing its more complex nanoscale organization by probing Argiope bruennichi dragline-type fibers using scanning X-ray nanodiffraction. This allows resolving transversal structural features such as an about 1 pm skin layer composed of around 100 nm diameter nanofibrils serving presumably as an elastic sheath. The core consists of a composite of several nm size crystalline nanodomains with poly(L-alanine) microstructure, embedded in a polypeptide network with Short-range order. Stacks of nanodomains separated by less ordered nanosegments form nanofibrils with a periodic axial density modulation which is particularly sensitive to radiation damage. The precipitation of larger beta-type nanocrystallites in the outer core shell is attributed to MaSp1 protein molecules.