Abstract
Topological structures of bio-architectonics and bio-interfaces play major roles in maintaining the normal functions of organs, tissues, extracellular matrix, and cells. In-depth understanding of natural self-assembly mechanisms and mimicking functional structures provide us opportunities to artificially control the natural assemblies and their biofunctions. Here, we report an intracellular enzyme-catalyzed polymerization approach for efficient synthesis of polypeptides and in situ construction of topology-controlled nanostructures. We reveal that the phase behavior and topological structure of polypeptides are encoded in monomeric peptide sequences. Next, we elucidate the relationship between polymerization dynamics and their temperature-dependent topological transition in biological conditions. Importantly, the linearly grown elastin-like polypeptides are biocompatible and aggregate into nanoparticles that exhibit significant molecular accumulation and retention effects. However, 3D gel-like structures with thermo-induced multi-directional traction interfere with cellular fates. These findings allow us to exploit new nanomaterials in living subjects for biomedical applications.
Highlights
Topological structures of bio-architectonics and bio-interfaces play major roles in maintaining the normal functions of organs, tissues, extracellular matrix, and cells
The modular monomeric peptide is composed of a functional molecule (i.e., 4-(2-carboxypyrrolidin1-yl)-7-(N,N-dimethylamino-sulphonyl)-2,1,3-benzoxadiazole (DBD), coumarin (CO), fluorescein isothiocyannate (FITC), cyanine 5.5 (Cy 5.5) or purpurin 18 (P18)), polymerization active sites (i.e., Q/K or QK/QK) and an elastin-based repeat unit (i.e., AVHPGVGP, HHPGVG, HDPGVG, HPGVGH, RLGVGFP, RLGVGLP, RLGVGDP, VHPGVG, VPHVG, and APGVG)
The polymerization process was monitored by fluorescence resonance energy transfer (FRET) method
Summary
Topological structures of bio-architectonics and bio-interfaces play major roles in maintaining the normal functions of organs, tissues, extracellular matrix, and cells. The TGase was used as an endogenous high-efficient catalyst[24, 35] to polymerize ELPs and fabricate thermal-induced topological controllable nanomaterials in cells Because of these properties, the enzyme-specific polymerization and sequent induced selfaggregation open a gate to spy upon the intracellular topological effect, further better understand the inherent topology of molecular/multimolecular interactions. Through rational design of the sequences, the polypeptides exhibit various physiochemical properties and phase transition behaviors, allowing us to build up a multi-dimensional approach to elucidate intracellular polymerization and the self-aggregation process. Based on this approach, various topological nanostructures are developed in situ in cytoplasm and found to exhibit variable biofunctions towards retention efficiency and cell cytotoxicity.
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