Mixing characterization inside microdroplets engineered on a microcoalescer

We use a microdevice where microdroplets of reagents are generated and coalesce in a carrier continuous phase. The work focuses on the characterization of the mixing step inside the droplets, in the perspective to use them for chemical kinetic data acquisition. A dye and water are used, and an acid–base instantaneous chemical reaction is monitored thanks to a colored indicator. Acquisitions are done with a high-speed camera coupled to a microscope and a mixing parameter is calculated by image analysis. Different angles of bended channels and different ways of coalescence are compared. It is shown that the homogenization of the droplets can be reached in less than 10 ms after coalescence. This is achieved by forcing the droplets to coalesce in a “shifted” way, and later by adding 45◦ angle bends along the channel

Speckle visibility spectroscopy and variable granular fluidization

We introduce a dynamic light scattering technique capable of resolving motion that changes systematically, and rapidly, with time. It is based on the visibility of a speckle pattern for a given exposure duration. Applying this to a vibrated layer of glass beads, we measure the granular temperature and its variation with phase in the oscillation cycle. We observe several transitions involving jammed states, where the grains are at rest during some portion of the cycle. We also observe a two-step decay of the temperature on approach to jamming.Comment: 4 pages, 4 figures, experimen

Quantum theory of dynamic multiple light scattering

We formulate a quantum theory of dynamic multiple light scattering in fluctuating disordered media and calculate the fluctuation and the autocorrelation function of photon number operator for light transmitted through a disordered slab. The effect of disorder on the information capacity of a quantum communication channel operating in a disordered environment is estimated and the use of squeezed light in diffusing-wave spectroscopy is discussed.Comment: Revised text, additional figur

Increased Biological Activity of Aneurinibacillus migulanus Strains Correlates with the Production of New Gramicidin Secondary Metabolites

Acknowledgments This project was funded by the Government of Kuwait (to FA) and the European Union Seventh Framework Programme under grant agreement 245268 (ISEFOR; to LB and SW). Further support came from the SwissBOL project, financed by the Swiss Federal Office for the Environment (grant holder LB) and the Sciex–Scientific Exchange Programme (http://nms.ch/) (NMS.CH; to LL and LB). LL is indebted to the Ministry of Education, Science, Research and Sport of the Slovak Republic for financial support in the frame of the project “VEGA 1/0061/16” and “VEGA 1/0046/16”. Funding This project was funded by the Government of Kuwait (to FA) and the European Union Seventh Framework Programme under grant agreement 245268 (ISEFOR; to LB and SW). Further support came from the SwissBOL project, financed by the Swiss Federal Office for the Environment (grant holder LB) and the Sciex–Scientific Exchange Programme NMS.CH (to LL and LB). LL is indebted to the Ministry of Education, Science, Research and Sport of the Slovak Republic for financial support in the frame of the project “VEGA 1/0061/16.”Peer reviewedPublisher PD

Nonlinear elasticity of stiff biopolymers connected by flexible linkers

Networks of the biopolymer actin, cross-linked by the compliant protein filamin, form soft gels. They can, however, withstand large shear stresses due to their pronounced nonlinear elastic behavior. The nonlinear elasticity can be controlled by varying the number of cross-links per actin filament. We propose and test a model of rigid filaments decorated by multiple flexible linkers that is in quantitative agreement with experiment. This allows us to estimate loads on individual cross-links, which we find to be less than 10 pN. © 2009 The American Physical Society

The Asp272-Glu282 Region of Platelet Glycoprotein Ib Interacts with the Heparin-binding Site of -Thrombin and Protects the Enzyme from the Heparin-catalyzed Inhibition by Antithrombin III

Platelet glycoprotein Ib (GpIb) mediates interaction with both von Willebrand factor and thrombin. Thrombin binds to GpIb via its heparin-binding site (HBS) (De Candia, E., De Cristofaro, R., De Marco, L., Mazzucato, M., Picozzi, M., and Landolfi, R. (1997) Thromb. Haemostasis 77, 735–740; De Cristofaro, R., De Candia, E., Croce, G., Morosetti, R., and Landolfi, R. (1998) Biochem. J. 332, 643–650). To identify the thrombin-binding domain on GpIbα, we examined the effect of GpIbα1–282, a GpIbα fragment released by the cobra venom mocarhagin on the heparin-catalyzed rate of thrombin inhibition by antithrombin III (AT). GpIbα1–282 inhibited the reaction in a dose-dependent and competitive fashion. In contrast, the GpIbα1–271 fragment, produced by exposing GpIbα1–282 to carboxypeptidase Y, had no effect on thrombin inhibition by the heparin-AT complex. Measurements of the apparent equilibrium constant of the GpIbα1–282 binding to thrombin as a function of different salts (NaCl and tetramethyl-ammonium chloride) concentration (0.1–0.2 M) indicated a large salt dependence (Γ± = −4.5), similar to that pertaining to the heparin binding to thrombin. The importance of thrombin HBS in its interaction with GpIbα was confirmed using DNA aptamers, which specifically bind to either HBS (HD22) or the fibrinogen recognition site of thrombin (HD1). HD22, but not HD1, inhibited thrombin binding to GpIbα1–282. Furthermore, the proteolytic derivative γT-thrombin, which lacks the fibrinogen recognition site, binds to GpIbα via its intact HBS in a reaction that is inhibited by HD22. Neither α- nor γT-thrombin bound to GpIbα1–271, suggesting that the Asp272–Glu282 region of GpIbα may act as a “heparin-like” ligand for the thrombin HBS, thereby inhibiting heparin binding to thrombin. It was also demonstrated that intact platelets may dose-dependently inhibit the heparin-catalyzed thrombin inhibition by AT at enzyme concentrations <5 nM. Altogether, these findings show that thrombin HBS binds to the region of GpIbα involving the Asp272–Glu282 segment, protecting the enzyme from the inactivation by the heparin-AT system