posted on 2022-09-26, 21:29authored byXuemin Chen, Yu Liu, Shuhua Yin, Jiachen Zang, Tuo Zhang, Chenyan Lv, Guanghua Zhao
Reversible sol–gel transforming
behaviors combined with
tunable mechanical properties are vital demands for developing biomaterials.
However, it remains challenging to correlate these properties with
the hydrogels constructed by denatured protein as building blocks.
Herein, taking advantage of naturally high-affinity coordination environments
consisting of i, i + 4 His-Glu motifs
offered by paramyosin, a ubiquitous nanofibrous protein, we found
that Zn2+ rather than Ca2+ or Mg2+ has the ability to trigger the self-assembly of native abalone paramyosin
(AbPM) into protein hydrogels under benign conditions, while the addition
of EDTA induces the hydrogels back into protein monomers, indicative
of a reversible process. By using such sol–gel reversible property,
the AbPM gels can serve as a vehicle to encapsulate bioactive molecules
such as curcumin, thereby protecting it from degradation from thermal
and photo treatment. Notably, based on the high conserved structure
of native AbPM, the mechanical property and biological activity of
the fabricated AbPM hydrogels can be fined-tuned by its noncovalent
interaction with small molecules. All these findings raise the possibility
that native paramyosin can be explored as a new class of protein hydrogels
which exhibit favorable properties that the traditional hydrogels
constructed by denatured protein building blocks do not have.