Generators of space-time dynamics in bioimaging have become essential to build ground truth datasets for image processing algorithm evaluation such as biomolecule detectors and trackers, as well as to generate training datasets for deep learning algorithms. In this contribution, we leverage a stochastic model, called birth-death-move (BDM) point process, in order to generate joint dynamics of biomolecules in cells. This particle-based stochastic simulation method is very flexible and can be seen as a generalization of well-established standard particle-based generators. In comparison, our approach allows us: (1) to model a system of particles in motion, possibly in interaction, that can each possibly switch from a motion regime (e.g., Brownian) to another (e.g., a directed motion); (2) to take into account finely the appearance over time of new trajectories and their disappearance, these events possibly depending on the cell regions but also on the current spatial configuration of all existing particles. This flexibility enables to generate more realistic dynamics than standard particle-based simulation procedures, by for example accounting for the colocalization phenomena often observed between intracellular vesicles. We explain how to specify all characteristics of a BDM model, with many practical examples that are relevant for bioimaging applications. As an illustration, based on real fluorescence microscopy datasets, we finally calibrate our model to mimic the joint dynamics of Langerin and Rab11 proteins near the plasma membrane, including the well-known colocalization occurrence between these two types of vesicles. We show that the resulting synthetic sequences exhibit comparable features as those observed in real microscopy image sequences.
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http://dx.doi.org/10.1017/S2633903X2300020X | DOI Listing |
J Phys Chem B
January 2025
Department of Physical Chemistry, Sciences II, University of Geneva, 30 Quai Ernest Ansermet, Geneva 1211, Switzerland.
The formation of protein condensates (droplets) via liquid-liquid phase separation (LLPS) is a commonly observed phenomenon in vitro. Changing the environmental properties with cosolutes, molecular crowders, protein partners, temperature, pressure, etc. has been shown to favor or disfavor the formation of protein droplets by fine-tuning the water-water, water-protein, and protein-protein interactions.
View Article and Find Full Text PDFJ Am Chem Soc
January 2025
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
NMR spectroscopy presents boundless opportunities for understanding the structure, dynamics, and function for a broad range of scientific applications. Solid-state NMR (SSNMR), in particular, provides novel insights into biological and material systems that are not amenable to other approaches. However, a major bottleneck is the extent of user training and the difficulty of obtaining reproducible, high-quality experimental results, especially for the sophisticated multidimensional pulse sequences that are essential to provide site-resolved measurements in large biomolecules.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
MOE Key Laboratory of Bio-Intelligent Manufacturing, Liaoning Key Laboratory of Molecular Recognition and Imaging, School of Bioengineering, Dalian University of Technology, Dalian 116023, PR China. Electronic address:
Surfaces capable of specific biomolecule recognition are essential for cancer theranostics, biosensing, and tissue engineering. However, current grafting methods, critical for dictating the recognition efficiency and biocompatibility of biomaterials, especially hydrophilic polymers, struggle to balance high grafting density with ease of implementation. In pursuit of a simple, effective, and versatile solution, we introduced a polydopamine (PDA)-assisted Ca-mediated grafting strategy using hyaluronic acid (HA) as a model material.
View Article and Find Full Text PDFNano Lett
January 2025
Department of Chemistry, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, South Korea.
Analyzing the cell interface is of paramount importance in understanding how cells interact and communicate with other cells, but an advanced analytical platform that can process complex and networked interactions between cell surface ligands and receptors is lacking. Herein, we developed the cell-interface-deciphering lipid nanotablet (CID-LNT) for multiplexed real-time cell analysis. LNT is a nanoparticle-tethered lipid bilayer chip where freely diffusing plasmonic nanoparticles induce scattering signal changes.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Single Molecule Analysis Group, Department of Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, United States.
Single-molecule fluorescence resonance energy transfer (smFRET) has emerged as a pivotal technique for probing biomolecular dynamics over time at nanometer scales. Quantitative analyses of smFRET time traces remain challenging due to confounding factors such as low signal-to-noise ratios, photophysical effects such as bleaching and blinking, and the complexity of modeling the underlying biomolecular states and kinetics. The dynamic distance information shaping the smFRET trace powerfully uncovers even transient conformational changes in single biomolecules both at or far from equilibrium, relying on trace idealization to identify specific interconverting states.
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