Humbolt squids are among the largest and fiercest animals in the ocean. They owe the latter distinction in part to their all protein sucker ring teeth. The sucker ring teeth protein (SRTP) of which there are many variations that form a composite-like material with strength comparable to Bombyx mori silk. However, unlike silk, SRTPs exhibit toughening when wet. Herein, we probe the mechanism of aqueous toughening as well as the role of salt anions on this process. Insoluble monolayers films of SRTP were formed by spin assisted deposition then crosslinked using horseradish peroxidase for mechanistic analysis. Structural changes characteristic of the toughening process is monitored via time-resolved high resolution atomic force microscopy and Fourier transform infrared spectroscopy. The rearrangement of nanoconfined crystalline regions is probed via X-ray diffraction. Observed surface and cross-sectional assembly are mapped with changes in mechanistic response characterized via buckling test for membrane mechanical analysis.

Aqueous toughening in crosslinked marine animal proteins

255th National Meeting (2018)

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