Based on the typical similar repeat units (abcdefg)
n
of α-helical structure, the peptide H
was
designed to self-assemble into an organohydrogel in response to pH.
Depending on the different pH, the proportions of secondary structure,
microstructure, and mechanical properties of the gel were investigated.
Circular dichroism (CD) and Fourier transform infrared (FT-IR) showed
that the proportion of α-helical structure gradually increased
to become dominant with the increase of pH. Combining transmission
electron microscopy (TEM) and atomic force microscopy (AFM), it was
found that the increase of the ordered α-helix structure promoted
fiber formation. The further increase in pH changed the intermolecular
forces, resulting in an increase in the α-helix content and
the enhancement of helix–helix interaction, causing the gel
fibers to converge into thicker and more dense ones. The temperature
test showed the stable rheological properties of the organohydrogel
between 20–60 °C. Drug release and cytotoxicity showed
that the DOX-loaded organohydrogel could have a better release in
an acidic environment, indicating its potential application as a drug
local delivery carrier.