Peptide
hydrogels are excellent candidates for medical therapeutics due to their tuneable viscoelastic
properties, however, in vivo they will be subject to various osmotic
pressures, temperature changes, and biological co-solutes, which could
alter their performance. Peptide hydrogels formed from the synthetic
peptide I3K have a temperature-induced hardening of their
shear modulus by a factor of 2. We show that the addition of uncross-linked
poly(N-isopropylacrylamide) chains to the peptide
gels increases the gels’ temperature sensitivity by 3 orders
of magnitude through the control of osmotic swelling and cross-linking.
Using machine learning combined with single-molecule fluorescence
microscopy, we measured the modulation of states of prestress in the
gels on the level of single peptide fibers. A new self-consistent
mixture model was developed to simultaneously quantify the energy
and the length distributions of the states of prestress. Switching
the temperature from 20 to 40 °C causes 6-fold increases in the
number of states of prestress. At the higher temperature, many of
the fibers experience constrained buckling with characteristic small
wavelength oscillations in their curvature.