Peroxidase-Mediated In Situ Fabrication of Multi-Stimuli-Responsive and Dynamic Protein Nanogels from Tyrosine-Conjugated Biodynamer and Ovablumin

Abstract

Horseradish peroxidase (HRP)-mediated oxidation of tyrosine-conjugated biodynamer containing acylhydrazone linkages and ovalbumin (OVA)/reduced ovalbumin (rOVA) generated protein nanogels through simultaneous tyrosine coupling and thiol cross-linking in the presence of H 2 O 2 . The obtained nanogels are multi-stimuli-responsive to temperature, pH, and glutathione (GSH) and possess the dynamic character of reversible covalent bonds. The OVAbased or rOVA-based protein nanogels can be utilized as cargoes of anticancer drug curcumin (Cur). The Cur-loaded protein nanogels rapidly released Cur in intracellularmimicking acidic and reductive environment, thus, making these protein nanogels promising nanocarriers for intracellular drug delivery. HRP-mediated cross-linking of the tyrosine-conjugated biodynamer and proteins provides a facile and versatile approach for fabrication of responsive and adaptive biohybrid nanogels under mild conditions.

Chemical Modification for the “Off‐/On” Regulation of Enzyme Activity

“…In addition, the phenol group of tyrosine can be easily activated to form the quinone or phenoxy radical, which enables a dynamic oxidoreductase response for the off/on control of enzyme activity. [ 23a ]…”

“…With the development of methods for protein chemical modification, Tyr and Trp residues and N termini have drawn much attention since the coupling reaction is bioorthogonal to other functional residues of proteins, such as lysine and carboxylate residues. [ 23 ] In general, although few strategies choose Tyr, Trp residues, and N termini as the chemical modification sites to construct a controllable enzyme activity system, they indeed provide some unique features and convenient methods in some cases. In addition, the phenol group of tyrosine can be easily activated to form the quinone or phenoxy radical, which enables a dynamic oxidoreductase response for the off/on control of enzyme activity.…”

Egg White Protein–Proanthocyanin Complexes Stabilized Emulsions: Investigation of Physical Stability, Digestion Kinetics, and Free Fatty Acid Release Dynamics

“…The incorporation of the proanthocyanins markedly augmented the synthesis of the dimeric tyrosine (Figure 1g). Within the redox milieu, the culmination of dimeric tyrosine formation was attributed to the existence of hydrogen peroxide [24]. Hydrogen peroxide catalytically fostered the covalent crosslinking, occurring intra-or intermolecularly amongst the proteins, via the direct oxidation of aromatic rings within two tyrosine molecules [25].…”

Polymer brush-based erasable and rewritable nanostructured particle surfaces

“…Dynamic covalent bonds, including disulfides, alkoxyamine, hydrazine and imine bonds, are widely used in the synthesis of smart materials. [15][16][17][18][19][20][21][22][23][24][25][26][27] With the rapid development of thiol chemistry, disulfides have found wide applications in materials science. [28][29][30][31] Disulfides can be formed through the oxidation of two thiol groups; meanwhile, the disulfides can be reduced to thiols by a reductant, resulting in the cleavage of the covalent bonds.…”