Emergence of a Promiscuous Peroxidase Under Non‐Equilibrium Conditions**

Abstract

Herein, we report the substrate induced generation of a transient catalytic microenvironment from a single amino acid functionalized fatty acid in presence of a cofactor hemin. The catalytic state accessed under non-equilibrium conditions showed acceleration of peroxidase activity resulting in degradation of the substrate and subsequently led to disassembly. Equilibrated systems could not access the three-dimensional microphases and showed substantially lower catalytic activity. Further, the assembled state showed latent catalytic function (promiscuity) to hydrolyze a precursor to yield the same substrate. Consequently, the assembly demonstrated protometabolism by exploiting the peroxidase-hydrolase cascade to augment the lifetime and the mechanical properties of the catalytic state.

Biomacromolecule‐Fueled Transient Volume Phase Transition of a Hydrogel

“…The chemically fueled transient volume phase transition (TVPT) of poly(methacrylic acid) microgels has been reported by the introduction of the CRN comprising carboxylic anhydride formation and water‐induced hydrolysis [40] . These chemical systems have also afforded chemically fueled transient payload release [40–43] and/or catalytic activity [44] . However, a polymer hydrogel that exhibits the transient structural change fueled by a biomacromolecule has not been reported.…”

Cross β Amyloid Nanotubes Demonstrate Promiscuous Catalysis in a Chemical Reaction Network via Co‐option

“…More versatility and promiscuity in the metabolic cycle are suggested to be connected to the enzymes being more evolvable [10] . Further, with promiscuous protoenzymes, nature had to invest in fewer rudimentary enzymes that could act on multiple substrates to access a diverse range of metabolic capabilities [11, 12] …”

“…[10] Further, with promiscuous protoenzymes, nature had to invest in fewer rudimentary enzymes that could act on multiple substrates to access a diverse range of metabolic capabilities. [11,12] The earliest rudimentary protein folds have been argued to be short peptides that can assemble in harsh conditions to access remarkably ordered para-crystalline folded structures. [13][14][15][16][17][18][19][20][21][22][23] Herein, we report the cross β assemblies of a short peptide that can demonstrate catalytic promiscuity to facilitate three metabolically relevant orthogonal chemical transformations (CÀ C and CÀ O bond cleavage and C=N bond condensation) and importantly, create a network that benefits the connected transformations.…”

Transient Biomacromolecular Nanoparticles for Labels with Self‐Erasable and Rewritable Ability

“…[45] Despite the progress in the field, the number of synthetic molecules for chemical fueldriven non-equilibrium self-assembly systems remains rather limited. [46][47][48][49][50] There were also some limitations in the synthesis of molecules for non-equilibrium self-assembly, including costand labor-consuming preparation, toxicity, and the difficulty to mass-produce. In comparison with synthetic molecules, natural polymers have the advantages of low cost, low toxicity, and sustainability.…”