Linothele
fallax
(Mello-Leitão)
(
L. fallax
) spider web, a potentially
attractive tissue engineering material, was investigated using quantitative
peak force measurement atomic force microscopy and scanning electron
microscopy with energy dispersive spectroscopy both in its natural
state and after treatment with solvents of different protein affinities,
namely, water, ethanol, and dimethyl sulfoxide (DMSO). Native
L. fallax
silk threads are densely covered by globular
objects, which constitute their inseparable parts. Depending on the
solvent, treating
L. fallax
modifies
its appearance. In the case of water and ethanol, the changes are
minor. In contrast, DMSO practically removes the globules and fuses
the threads into dense bands. Moreover, the solvent treatment influences
the chemistry of the threads’ surface, changing their adhesive
and, therefore, biocompatibility and cell adhesion properties. On
the other hand, the solvent-treated web materials’ contact
effect on different types of biological matter differs considerably.
Protein-rich matter controls humidity better when wrapped in spider
silk treated with more hydrophobic solvents. However, carbohydrate
plant materials retain more moisture when wrapped in native spider
silk. The extracts produced with the solvents were analyzed using
nuclear magnetic resonance (NMR) and liquid chromatography–mass
spectrometry techniques, revealing unsaturated fatty acids as representative
adsorbed species, which may explain the mild antibacterial effect
of the spider silk. The extracted metabolites were similar for the
different solvents, meaning that the globules were not “dissolved”
but “fused into” the threads themselves, being supposedly
rolled-in knots of the protein chain.