Intracellular aggregations of biological elements: From simple to complex

Abstract

Most cellular elements could be functioned by forming aggregate structures through interactions with other molecules, which is like the luminescence mechanism of AIE molecules. However, in comparison to AIE molecules, the aggregation of biological elements appears to be more complex due to membership and mechanism, which is in line with the trend in biological evolution following the principle of simplicity to complexity. Here, we chose three distinctive examples because they differ significantly in their composition and show a progression from simple to complex, namely protein–protein complexes, protein–nucleic acid complexes, and protein–nucleic acid–lipid complexes. The majority of units that perform functions within cells belong to these three types. We discuss the formation mechanisms and related functions of the protein–protein complex (PML‐NB), the proteins–nucleic acids complex ribosome, and the proteins–nucleic acids–lipids complex exosome, and hope to provide expert insight for related fields.

High-Fidelity Assay Based on Turn-Off Fluorescence to Detect the Perturbations of Cellular Proteostasis

“…To visualize perturbations to the homeostasis of the proteome (proteostasis), many methods have been established in recent years. − Among them, our lab has developed AgHalo and AggTag technologies, − which rely on the utility of solvatochromic , and molecular-rotor based fluorophores − to differentiate between changes in the polarity and viscosity of the local microenvironment. − In these applications, the rigidity and hydrophobicity of misfolded oligomeric and aggregate species yield an increase in fluorescence intensity relative to the soluble, native conformation of the protein-probe conjugate. Together the AggTag and AgHalo systems are effective methodologies to visualize the onset of proteomic stress (Figure a).…”

Solvatochromic sensors detect proteome aggregation in stressed liver tissues with hepatic cancer and cirrhosis

“…To date, it is still challenging to detect and dissect protein aggregates formed in cellular environments, nevertheless its biological significance.Very limited chemical tools are applicable for observing the occurrence of the aggregated proteome in cells and tissues due to the lack of 3-dimensional conformations and recognition sites for the rational design of chemical probes. 8,9 Tang, Zhu, and Cui developed fluorophores (such as aggregation induced emission (AIE) molecules) to detect extracellular amyloid plaques and fibrils. [10][11][12][13][14][15][16][17][18] Hong and Hatters reported the first chemical strategy to depict the proteome unfolding process inside the cellular milieu via the covalent labeling of maleimide…”