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Updated: Jul 31, 2025
4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Real-time imaging of sulfhydryl single-stranded DNA aggregation
Fanwei Zeng1, Youhong Jiang1, Nana He1
1State Key Laboratory of Physical Chemistry of Solid Surfaces, Collaborative Innovation Center of Chemistry for Energy Materials, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China.
Abstract:
The structure and functionality of biomacromolecules are often regulated by chemical bonds, however, the regulation process and underlying mechanisms have not been well understood. Here, by using in situ liquid-phase transmission electron microscopy (LP-TEM), we explored the function of disulfide bonds during the self-assembly and structural evolution of sulfhydryl single-stranded DNA (SH-ssDNA). Sulfhydryl groups could induce self-assembly of SH-ssDNA into circular DNA containing disulfide bonds (SS-cirDNA). In addition, the disulfide bond interaction triggered the aggregation of two SS-cirDNA macromolecules along with significant structural changes. This visualization strategy provided structure information at nanometer resolution in real time and space, which could benefit future biomacromolecules research.
