Optical manipulation of a dielectric particle along polygonal closed-loop geometries within a single water droplet

We report a new method to optically manipulate a single dielectric particle along closed-loop polygonal trajectories by crossing a suite of all-fiber Bessel-like beams within a single water droplet. Exploiting optical radiation pressure, this method demonstrates the circulation of a single polystyrene bead in both a triangular and a rectangle geometry enabling the trapped particle to undergo multiple circulations successfully. The crossing of the Bessel-like beams creates polygonal corners where the trapped particles successfully make abrupt turns with acute angles, which is a novel capability in microfluidics. This offers an optofluidic paradigm for particle transport overcoming turbulences in conventional microfluidic chips.

Polarized SERS Controlled by Anisotropic Growth on Ordered Curvature Substrate

Colloidal lithography is an efficient and low-cost method to prepare an ordered nanostructure array with new shapes and properties. In this study, square-shaped and cone-shaped Au nanostructures were obtained by 70° angle deposition onto polystyrene bead array with the diameter of 500 nm when a space of 120 nm is created between the neighbor beads by plasma etching. The gaps between the units decrease when the Au deposition time increases, which leads to the polarized enhanced local field, in agreement with the surface-enhanced Raman scattering spectra (SERS) observations and finite-difference time-domain (FDTD) simulations. When the Au deposition time increased to 5 min, 5 nm gaps form between the neighbor units, which gave an enhancement factor of 5 × 109. The SERS chip was decorated for the detection of the liver cancer cell marker Alpha-fetoprotein (AFP) with the detection limit down to 5 pg/mL.

Novel amiloride derivatives that inhibit bacterial motility across multiple strains and stator types

The bacterial flagellar motor (BFM) is a protein complex that confers motility to cells and contributes to survival and virulence. The BFM consists of stators that are ion-selective membrane protein complexes and a rotor that directly connects to a large filament, acting as a propeller. The stator complexes couple ion transit across the membrane to torque that drives rotation of the motor. The most common ion gradients that drive BFM rotation are protons (H+) and sodium ions (Na+). The sodium-powered stators, like those in the PomAPomB stator complex of Vibrio spp, can be inhibited by sodium channel inhibitors, in particular, by phenamil, a potent and widely used inhibitor. However, relatively few new sodium-motility inhibitors have been described since the discovery of phenamil. In this study, we discovered two motility inhibitors HM2-16F and BB2-50F from a small library of previously reported amiloride derivatives. Using a tethered cell assay, we showed that both HM2-16F and BB2-50F had inhibition comparable to that of phenamils on Na+ driven motors at matching concentrations, with an additional ability to inhibit rotation in H+ driven motors. The two compounds did not exhibit adverse effects on bacterial growth at the motility-inhibiting concentration of 10 uM, however toxicity was seen for BB2-50F at 100 uM. We performed higher resolution measurements to examine rotation inhibition at moderate (1 um polystyrene bead) and low loads (60 nm gold bead) and in both the presence and absence of stators. These measurements suggested that the compounds did not inhibit rotation via direct association with the stator, in contrast to the established mode of action of phenamil. Overall, HM2-16F and BB2-50F showed reversible inhibition of motility across a range of loads, in both Na+ and H+ stator types, and in pathogenic and non-pathogenic strains.

Altered N-glycan composition impacts flagella-mediated adhesion in Chlamydomonas reinhardtii

For the unicellular alga Chlamydomonas reinhardtii, the presence of N-glycosylated proteins on the surface of two flagella is crucial for both cell-cell interaction during mating and flagellar surface adhesion. However, it is not known whether only the presence or also the composition of N-glycans attached to respective proteins is important for these processes. To this end, we tested several C. reinhardtii insertional mutants and a CRISPR/Cas9 knockout mutant of xylosyltransferase 1A, all possessing altered N-glycan compositions. Taking advantage of atomic force microscopy and micropipette force measurements, our data revealed that reduction in N-glycan complexity impedes the adhesion force required for binding the flagella to surfaces. This results in impaired polystyrene bead binding and transport but not gliding of cells on solid surfaces. Notably, assembly, intraflagellar transport, and protein import into flagella are not affected by altered N-glycosylation. Thus, we conclude that proper N-glycosylation of flagellar proteins is crucial for adhering C. reinhardtii cells onto surfaces, indicating that N-glycans mediate surface adhesion via direct surface contact.

Microparticle manipulation using laser-induced thermophoresis and thermal convection flow

We demonstrate manipulation of microbeads with diameters from 1.5 to 10 µm and Jurkat cells within a thin fluidic device using the combined effect of thermophoresis and thermal convection. The heat flow is induced by localized absorption of laser light by a cluster of single walled carbon nanotubes, with no requirement for a treated substrate. Characterization of the system shows the speed of particle motion increases with optical power absorption and is also affected by particle size and corresponding particle suspension height within the fluid. Further analysis shows that the thermophoretic mobility (DT) is thermophobic in sign and increases linearly with particle diameter, reaching a value of 8 µm2 s−1 K−1 for a 10 µm polystyrene bead.

Altered N-glycan composition impacts flagella mediated adhesion in Chlamydomonas reinhardtii

For the unicellular alga Chlamydomonas reinhardtii, the presence of N-glycosylated proteins on the surface of two flagella is crucial for both cell-cell interaction during mating and flagellar surface adhesion. It is unknown whether the composition of N-glycans attached to respective proteins is important for these processes. To this end, we examined several C. reinhardtii insertional mutants and a CRIPSR/Cas9 knockout mutant of xylosyltransferase 1A, all possessing altered N-glycan compositions. Taking advantage of atomic force microscopy and micropipette force measurements, our data revealed that reduction in N-glycan complexity impedes the adhesion force required for binding the flagella to surfaces. In addition, polystyrene bead binding and transport is impaired. Notably, assembly, Intraflagellar Transport and FMG-1B transport into flagella are not affected by altered N-glycosylation. Thus, we conclude that proper N-glycosylation of flagellar proteins is crucial for adhering C. reinhardtii cells onto surfaces, indicating that N-glycans mediate surface adhesion via direct surface contact.