Construction of Sol-Gel Phase-Reversible Hydrogels with Tunable Properties with Native Nanofibrous Protein as Building Blocks.

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 Zn 2+ rather than Ca 2+ or Mg 2+ 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.