The authors report optical observations of the change in the dynamics of one and the same ultrasound contrast agent microbubble due to the influence of interfaces and neighboring bubbles. The bubble is excited by a 2.25MHz ultrasound burst and its oscillations are recorded with an ultrahigh-speed camera at 15 million frames per second. The position of an individual bubble relative to a rigid wall or second bubble is precisely controlled using optical tweezers based on Laguerre-Gaussian laser beams [P. Prentice et al., Opt. Express 12, 593 (2004); V. Garbin et al., Jpn. J. Appl. Phys. 44, 5773 (2005)]. This allows for repeated experiments on the very same bubble and for a quantitative comparison of the effect of boundaries on bubble behavior.

One of the emerging technologies in molecular diagnostics of the last two decades is the use of gold nanoparticles (AuNPs) for biosensors. AuNPs can be functionalized with various biomolecules, such as nucleic acids or antibodies, to recognize and bind to specific targets. AuNPs present unique optical properties, such as their distinctive plasmonic band, which confers a bright-red color to AuNP solutions, and their extremely high extinction coefficient, which makes AuNPs detectable by the naked eye even at low concentrations. Ingenious molecular mechanisms triggered by the presence of a target analyte can change the colloidal status of AuNPs from dispersed to aggregated, with a subsequent visible change in color of the solution due to the loss of the characteristic plasmonic band. This review describes how the optical properties of AuNPs have been exploited for the design of plasmonic biosensors that only require the simple mixing of reagents combined with a visual readout and focuses on the molecular mechanisms involved. This review illustrates selected examples of AuNP-based plasmonic biosensors and promising approaches for the point-of-care testing of various analytes, spanning from the viral RNA of SARS-CoV-2 to the molecules that give distinctive flavor and color to aged whisky.

During neuronal differentiation, lamellipodia and filopodia explore the environment in search for the correct path to the axon's final destination. Although the motion of lamellipodia and filopodia has been characterized to an extent, little is known about the force they exert. In this study, we used optical tweezers to measure the force exerted by filopodia and lamellipodia with a millisecond temporal resolution. We found that a single filopodium exerts a force not exceeding 3 pN, whereas lamellipodia can exert a force up to 20 pN. Using metabolic inhibitors, we showed that no force is produced in the absence of actin polymerization and that development of forces larger than 3 pN requires microtubule polymerization. These results show that actin polymerization is necessary for force production and demonstrate that not only do neurons process information, but they also act on their environment exerting forces varying from tenths pN to tens of pN.

Ingestion is the preferred way for drug administration. However, many drugs have poor oral bioavailability, warranting the use of injections. Extracellular vesicles (EVs) from cow milk have shown potential utility in improving oral drug bioavailability. However, EVs produced by intestinal epithelial cells have not been investigated for this application. We compared the capacity of cow milk EVs and intestinal epithelial cell-derived counterparts to enhance oral drug bioavailability. EVs were isolated, fluorescently labelled, and loaded with curcumin (CUR) as a model poorly absorbable drug. These were then characterised before testing in an intestinal model (Caco-2). Epithelial cell-derived EVs showed notably higher cell uptake compared to cow milk EVs. Cell uptake was significantly higher in differentiated compared to undifferentiated cells for both types of EVs. While both milk- and cell-derived EVs improved the cell uptake and intestinal permeability of CUR (confirming oral drug bioavailability enhancement potential), epithelial cell EVs demonstrated a superior effect.

Generally, the high diversity of protein properties necessitates the development of unique nanoparticle bio-conjugation methods, optimized for each different protein. Here we describe a universal bio-conjugation approach which makes use of a new recombinant fusion protein combining two distinct domains. The N-terminal part is Glutathione S-Transferase (GST) from Schistosoma japonicum, for which we identify and characterize the remarkable ability to bind gold nanoparticles (GNPs) by forming gold–sulfur bonds (Au–S). The C-terminal part of this multi-domain construct is the SpyCatcher from Streptococcus pyogenes, which provides the ability to capture recombinant proteins encoding a SpyTag. Here we show that SpyCatcher can be immobilized covalently on GNPs through GST without the loss of its full functionality. We then show that GST-SpyCatcher activated particles are able to covalently bind a SpyTag modified protein by simple mixing, through the spontaneous formation of an unusual isopeptide bond.