posted on 2023-12-26, 23:04authored byHonglei Lu, Xuejiao Yang, Huaimin Wang
The
molecular chaperones are essential and play significant roles
in controlling the protein phase transition and maintaining physiological
homeostasis. However, manipulating phase transformation in biomimetic
peptide self-assembly is still challenging. This work shows that an
artificial chaperone modulates the energy landscape of supramolecular
polymerization, thus controlling the phase transition of amyloid-like
assemblies from crystals to hydrogels to solution. The absence of
a chaperone allows the NapP to form crystals, while the
presence of the chaperone biases the pathway to form nanofibrous hydrogels
to soluble oligomers by adjusting the chaperone ratios. Mechanistic
studies reveal that the aromatic–aromatic interaction is the
key to trapping the molecules in a higher energy fold. Adding the
chaperone relieves this restriction, lowers the energy barrier, and
transforms the crystal into a hydrogel. This phase transformation
can also be achieved in the macromolecular crowding environment, thus
providing new insights into understanding molecular self-assembly
in multiple component systems.