Biology also uses post-translation modification to increase the diversity and functionality of these materials, which has inspired attaching various other types of polymers to biomacromolecules.
Proteins, nucleic acids, lipid vesicles, and carbohydrates are the major classes of biomacromolecules that function to sustain life.
It is desired to seek approaches for biological remediation of uranyl ions, and ultimately make a full use of the double-edged sword of uranium. These advances shed light on the structure-function relationship of proteins, especially for metalloproteins, as impacted by uranyl–protein interactions. Photo-induced protein/DNA cleavages, as well as other impacts, are also highlighted. Instead of focusing only on the structural information, this article aims to review the recent advances in understanding the binding of uranyl to proteins in either potential, native, or artificial metal-binding sites, and the structural-functional impacts of uranyl–protein interactions, such as inducing conformational changes and disrupting protein-protein/DNA/ligand interactions. Although uranyl–protein/DNA interactions have been known for decades, fewer advances are made in understanding their structural-functional impacts.
The widespread use of uranium for civilian purposes causes a worldwide concern of its threat to human health due to the long-lived radioactivity of uranium and the high toxicity of uranyl ion (UO22+). Here, the authors report development of living fabrication of biohybrid semi interpenetrating polymer networks by encapsulating protein producing bacteria within polymer microcapsules. Cell based materials production has potential for generating diverse materials with a range of functions. Our work lays the foundation for programming functional living materials for diverse applications. We demonstrate the adoption of the platform to protect gut microbiota in animals from antibiotic-mediated perturbations. The material is resilient to perturbations because of the continual assembly of the protein mesh from the monomers released by the engineered bacteria. The formation of sIPN serves the dual purposes of enhancing the mechanical property of the living materials and anchoring effector proteins for diverse applications. Those protein monomers polymerize with each other to form the second polymeric component that is interlaced with the initial crosslinked polymeric scaffold. The bacteria grow and undergo programmed lysis in a density-dependent manner, releasing protein monomers decorated with reactive tags. The fabrication process is driven by the engineered bacteria encapsulated in a polymeric microcapsule, which serves as the initial scaffold. Here, we demonstrate the engineering of living materials consisting of semi-interpenetrating polymer networks (sIPN).
Cell-mediated living fabrication has great promise for generating materials with versatile, programmable functions.