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The determination of in situ structural information of soft matter under flow is challenging, as it depends on many factors, such as temperature, concentration, confinement, channel geometry, and type of imposed flow. Here, we combine microfluidics and scanning small-angle X-ray scattering (scanning-SAXS) to create a two-dimensional spatially resolved map, which represents quantitatively the variation of molecular properties under flow. As application examples, mappings of confined amyloid fibrils and wormlike micelles under flow into various channel geometries are compared. A simple process to fabricate X-rays resistant chips, based on polyimide and UV-curing resin, is discussed. During experiments, these chips remained in high-energy synchrotron radiation for more than 24 hours, causing constant low background scattering. Thus, sufficient statistics were obtained from sample scattering at exposure times as low as 0.1 s, even with the small scattering volumes in microfluidic channels. Scanning-SAXS of microfluidic flows has many potential applications from biology to fundamental soft matter physics. In general, any fluid which has enough contrast for X-ray scattering can be measured to obtain the dependence of molecular shape, conformation, alignment and size on the flow field. Besides, dynamic processes of soft matter caused by flow, temperature, concentration gradient, and confinement, for example self-assembling, aggregation, mixing, diffusion, and disintegration of macromolecules, can be quantified and visualized on a single image by this mapping technique.
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http://dx.doi.org/10.1039/c6lc00690f | DOI Listing |
Anal Bioanal Chem
September 2025
School of Artificial Intelligence, Hangzhou Dianzi University, Hangzhou, 310018, China.
The prompt and accurate identification of pathogenic bacteria is crucial for mitigating the transmission of infections. Conventional detection methods face limitations, including lengthy processing, complex sample pretreatment, high instrumentation costs, and insufficient sensitivity for rapid on-site screening. To address these challenges, an aptamer (Apt)-sensor based on functionalized magnetic nanoparticles (MNPs) was developed for detecting Escherichia coli.
View Article and Find Full Text PDFBiomaterials
September 2025
State Key Laboratory of Chemical Resource Engineering, Beijing Advanced Innovation Center for Soft Matter Science and Engineering, Beijing University of Chemical Technology, Beijing, 100029, PR China. Electronic address:
Phys Rev Lett
August 2025
Laboratoire de Physique Théorique de la Matière Condensée, Sorbonne Université, CNRS, 75005 Paris, France.
We investigate nonreciprocal XY (NRXY) models defined on two-dimensional lattices in which the coupling strength of a spin with its neighbors varies with their position in the frame defined by the current spin orientation. As expected from the seminal work of Dadhichi et al., [Nonmutual torques and the unimportance of motility for long-range order in two-dimensional flocks, Phys.
View Article and Find Full Text PDFSoft Robot
September 2025
Bioinspired Soft Robotics Laboratory, Istituto Italiano di Tecnologia, Genoa, Italy.
Animal diaphragm-lung systems are soft organs that generate a controllable vacuum. Elephants, as rare land animals, can manipulate all three states of matter using their lung-generated vacuum. In soft robotics, however, current vacuum generation relies on rigid components, and no single soft device effectively handles all states of matter.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
September 2025
State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.
High-mobility group box protein 1 (HMGB1) is a chromatin-associated nonhistone protein widely distributed in the nucleus of eukaryotic cells. It is transported extracellularly as a proinflammatory mediator or late warning protein to induce immune and inflammatory reactions upon stimuli such as microbial infection. Here, we have found that HMGB1 directly interacts with bacterial DNA analogue CpG-A in the extracellular environment to undergo liquid-liquid phase separation (LLPS) via its positively charged DNA-binding domain.
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