A detailed insight about the molecular organization behind
spider
silk assembly is valuable for the decoding of the unique properties
of silk. The recombinant partial spider silk protein 4RepCT contains
four poly-alanine/glycine-rich repeats followed by an amphiphilic
C-terminal domain and has shown the capacity to self-assemble into
fibrils on hydrophobic surfaces. We herein use molecular dynamic simulations
to address the structure of 4RepCT and its different parts on hydrophobic
versus hydrophilic surfaces. When 4RepCT is placed in a wing arrangement
model and periodically repeated on a hydrophobic surface, β-sheet
structures of the poly-alanine repeats are preserved, while the CT
part is settled on top, presenting a fibril with a height of ∼7
nm and a width of ∼11 nm. Both atomic force microscopy and
cryo-electron microscopy imaging support this model as a possible
fibril formation on hydrophobic surfaces. These results contribute
to the understanding of silk assembly and alignment mechanism onto
hydrophobic surfaces.
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