Controlling the motion of small objects in suspensions wirelessly is of fundamental interest and has potential applications in biomedicine for drug delivery and micromanipulation of small structures. Here we show that magnetic helical microstructures that propel themselves in the presence of rotating weak magnetic fields assemble into various configurations that exhibit locomotion and a change in swimming direction. The configuration is tuned dynamically, that is, assembly and disassembly occur, by the field input. We investigate a system that consists of two identical right-handed helices assembled at their center in order to model the motion of assembled swimmers. The swimming properties are dependent on both the component design and the assembly configuration. For particular designs and configurations, a reversal in swimming direction emerges, yet with other designs, a reversal in motion never appears. Understanding the locomotion of clustered chiral structures enables uni- and multidirectional navigation of this class of active suspensions.
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J Am Chem Soc
January 2025
Center for Sustainable Materials (SusMat), School of Materials Science and Engineering, Nanyang Technological University, Singapore 639798, Singapore.
Complex coacervation is a form of liquid-liquid phase separation, whereby two types of macromolecules, usually bearing opposite net charges, self-assemble into dense microdroplets driven by weak molecular interactions. Peptide-based coacervates have recently emerged as promising carriers to deliver large macromolecules (nucleic acids, proteins and complex thereof) inside cells. Thus, it is essential to understand their assembly/disassembly mechanisms at the molecular level in order to tune the thermodynamics of coacervates formation and the kinetics of cargo release upon entering the cell.
View Article and Find Full Text PDFCurr Opin Neurobiol
January 2025
Department of Pathology & Cell Biology, Columbia University Irving Medical Center, 10032, New York, NY, USA. Electronic address:
Neurons are equipped with microtubules of different stability with stable and dynamic domains often coexisting on the same microtubule. While dynamic microtubules undergo random transitions between disassembly and assembly, stable ones persist long enough to serve as platforms for tubulin-modifying enzymes (known as writers) that attach molecular components to the α- or β-tubulin subunits. The combination of these posttranslational modifications (PTMs) results in a "tubulin code," dictating the behavior of selected proteins (known as readers), some of which were shown to be crucial for neuronal function.
View Article and Find Full Text PDFViruses
December 2024
Department of Microbiology and Immunology, Penn State College of Medicine, Hershey, PA 17033, USA.
Since the discovery of the Australia antigen, now known as the hepatitis B surface antigen (HBsAg), significant research has been conducted to elucidate its physical, chemical, structural, and functional properties. Subviral particles (SVPs) containing HBsAg are highly immunogenic, non-infectious entities that have not only revolutionized vaccine development but also provided critical insights into HBV immune evasion and viral assembly. Recent advances in cryo-electron microscopy (cryo-EM) have uncovered the heterogeneity and dynamic nature of spherical HBV SVPs, emphasizing the essential role of lipid-protein interactions in maintaining particle stability.
View Article and Find Full Text PDFTrends Cell Biol
January 2025
Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany. Electronic address:
The dynamic turnover of actin filaments drives the morphogenesis and migration of all eukaryotic cells. This review summarizes recent insights into the molecular mechanisms of actin polymerization and disassembly obtained through high-resolution structures of actin filament assemblies. We first describe how, upon polymerization, actin subunits age within the filament through changes in their associated adenine nucleotide.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Harvard John A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts 02138, United States.
In many simple viruses and virus-like particles, the protein capsid self-assembles around a nucleic-acid genome. Although the assembly process has been studied in detail, relatively little is known about how the capsid disassembles, a potentially important step for infection (in viruses) or cargo delivery (in virus-like particles). We investigate capsid disassembly using a coarse-grained molecular dynamics model of a = 1 dodecahedral capsid and an RNA-like polymer.
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