Nanovalve activation by surface-attached photoacids.
Ontology highlight
ABSTRACT:
SUBMITTER: Guardado-Alvarez TM
PROVIDER: S-EPMC4327900 | biostudies-literature | 2014 Aug
REPOSITORIES: biostudies-literature
Publications
Nanovalve activation by surface-attached photoacids.
Guardado-Alvarez T M TM Russell M M MM Zink J I JI
Chemical communications (Cambridge, England) 20140801 61
Proton transfer caused by excitation of a photoacid attached to the surface of a mesoporous silica nanoparticle activates a nanovalve and causes release of trapped molecules. The protonation of an aniline-based stalk releases a noncovalently bound cyclodextrin molecule that blocked a pore. The results show that pH-responsive molecular delivery systems can be externally controlled using light. ...[more]
Similar Datasets
Project description:Surface-attached, degradable polymer hydrogels with potential antimicrobial activity are reported. They were obtained by ring-opening metathesis copolymerization (ROMP) of a monomer with potential bioactivity and a monomer that carries a benzophenone cross-linker and a hydrolyzable group. The hydrolyzable group was either an ester or an anhydride group. The copolymers thus obtained were spin-coated onto silicon wafers and UV-irradiated to induce C,H cross-linking of the benzophenone groups and obtain the target polymer networks. Immersion of these networks into aqueous media triggered network degradation. The degradation speed depended on the nature of the intended break points (ester or anhydride groups), the number of cross-links per polymer chain, and the surrounding medium. By releasing bioactive polymer fragments to the medium ("leaching") and by regenerating the hydrogel surface during the degradation process, the hydrogels potentially have two ways to prevent biofilm formation on their surface.
| S-EPMC7611506 | biostudies-literature
Project description:A universal label-free method for the spectroscopic investigation of polyhistidine-tagged proteins is presented. A solid supported lipid bilayer (SSLB, picture) containing nitrilotriacetic-acid-modified lipids is attached on top of a germanium attenuated total reflection crystal by hydrophilic interactions. Any His tag-modified protein can be immobilized and investigated by FTIR spectroscopy.
| S-EPMC3531609 | biostudies-literature
Project description:Staphylococcus aureus is a prominent bacterial pathogen that causes a diverse range of acute and chronic infections. Recently, it has been demonstrated that the secreted nuclease (Nuc) enzyme is a virulence factor in multiple models of infection, and in vivo expression of nuc has facilitated the development of an infection imaging approach based on Nuc-activatable probes. Interestingly, S. aureus strains encode a second nuclease (Nuc2) that has received limited attention. With the growing interest in bacterial nucleases, we sought to characterize Nuc2 in more detail through localization, expression, and biochemical studies. Fluorescence microscopy and alkaline phosphatase localization approaches using Nuc2-GFP and Nuc2-PhoA fusions, respectively, demonstrated that Nuc2 is membrane bound with the C-terminus facing the extracellular environment, indicating it is a signal-anchored Type II membrane protein. Nuc2 enzyme activity was detectable on the S. aureus cell surface using a fluorescence resonance energy transfer (FRET) assay, and in time courses, both nuc2 transcription and enzyme activity peaked in early logarithmic growth and declined in stationary phase. Using a mouse model of S. aureus pyomyositis, Nuc2 activity was detected with activatable probes in vivo in nuc mutant strains, demonstrating that Nuc2 is produced during infections. To assess Nuc2 biochemical properties, the protein was purified and found to cleave both single- and double-stranded DNA, and it exhibited thermostability and calcium dependence, paralleling the properties of Nuc. Purified Nuc2 prevented biofilm formation in vitro and modestly decreased biomass in dispersal experiments. Altogether, our findings confirm that S. aureus encodes a second, surface-attached and functional DNase that is expressed during infections and displays similar biochemical properties to the secreted Nuc enzyme.
| S-EPMC3994088 | biostudies-literature
Project description:Heterotrophic microbes are central to organic matter degradation and transformation in marine sediments. Currently, most investigations of benthic microbiomes do not differentiate between processes in the porewater and on the grains and, hence, only show a generalized picture of the community. This limits our understanding of the structure and functions of sediment microbiomes. To address this problem, we fractionated sandy surface sediment microbial communities from a coastal site in Isfjorden, Svalbard, into cells associated with the porewater, loosely attached to grains, and firmly attached to grains; we found dissimilar bacterial communities and metabolic activities in these fractions. Most (84%-89%) of the cells were firmly attached, and this fraction comprised more anaerobes, such as sulfate reducers, than the other fractions. The porewater and loosely attached fractions (3% and 8%-13% of cells, respectively) had more aerobic heterotrophs. These two fractions generally showed a higher frequency of dividing cells, polysaccharide (laminarin) hydrolysis rates, and per-cell O2 consumption than the firmly attached cells. Thus, the different fractions occupy distinct niches within surface sediments: the firmly attached fraction is potentially made of cells colonizing areas on the grain that are protected from abrasion, but might be more diffusion-limited for organic matter and electron acceptors. In contrast, the porewater and loosely attached fractions are less resource-limited and have faster growth. Their cell numbers are kept low possibly through abrasion and exposure to grazers. Differences in community composition and activity of these cell fractions point to their distinct roles and contributions to carbon cycling within surface sediments.
| S-EPMC11368169 | biostudies-literature
Project description:With the risks associated with healthcare-associated infections and the rise of antibiotic resistant microorganisms, there is an important need to control the proliferation of these factors in hospitals, retirement homes and other institutions. This work explores the development and application of a novel class of sulfonamide-based quaternary ammonium antimicrobial coatings, anchored to commercially and clinically relevant material surfaces. Synthesized in high yields (60-97%), benzophenone-anchored antimicrobials were spray-coated and UV grafted onto plastic surfaces, while silane-anchored variants were adhered to select textiles via dip-coating. Surface modified samples were characterised by advancing contact angle, anionic dye staining, X-ray photoelectron spectroscopy and atomic force microscopy. After verifying coating quality through the above characterization methods, microbiological testing was performed on batch samples in conditions that simulate the natural inoculation of surfaces and objects (solid/air) and water containers (solid/liquid). Using the previously established Large Drop Inoculum (LDI) protocol at solid/air interfaces, all treated samples showed a full reduction (105-107 CFU) of viable Arthrobacter sp., S. aureus, and E. coli after 3 h of contact time. Additional testing of the walls of plastic LDPE vials treated with a UV-cured sulfonamide antimicrobial at a solid/liquid interface using the newly developed Large Reservoir Inoculum (LRI) protocol under static conditions revealed a complete kill (>106 reduction) of Gram-positive Arthrobacter sp., and a partial kill (>104 reduction) of Gram-negative E. coli within 24-48 h of contact.
| S-EPMC9059942 | biostudies-literature
Project description:Bacteria use a process called quorum sensing to communicate and orchestrate collective behaviours, including virulence factor secretion and biofilm formation. Quorum sensing relies on the production, release, accumulation and population-wide detection of signal molecules called autoinducers. Here, we develop concepts to coat surfaces with quorum-sensing-manipulation molecules as a method to control collective behaviours. We probe this strategy using Staphylococcus aureus. Pro- and anti-quorum-sensing molecules can be covalently attached to surfaces using click chemistry, where they retain their abilities to influence bacterial behaviours. We investigate key features of the compounds, linkers and surfaces necessary to appropriately position molecules to interact with cognate receptors and the ability of modified surfaces to resist long-term storage, repeated infections, host plasma components and flow-generated stresses. Our studies highlight how this surface approach can be used to make colonization-resistant materials against S. aureus and other pathogens and how the approach can be adapted to promote beneficial behaviours of bacteria on surfaces.
| S-EPMC5526357 | biostudies-literature
Project description:Bacteria inhabit a wide variety of environments in which fluid flow is present, including healthcare and food processing settings and the vasculature of animals and plants. The motility of bacteria on surfaces in the presence of flow has not been well characterized. Here we focus on Pseudomonas aeruginosa, an opportunistic human pathogen that thrives in flow conditions such as in catheters and respiratory tracts. We investigate the effects of flow on P. aeruginosa cells and describe a mechanism in which surface shear stress orients surface-attached P. aeruginosa cells along the flow direction, causing cells to migrate against the flow direction while pivoting in a zig-zag motion. This upstream movement is due to the retraction of type IV pili by the ATPase motors PilT and PilU and results from the effects of flow on the polar localization of type IV pili. This directed upstream motility could be beneficial in environments where flow is present, allowing bacteria to colonize environments that cannot be reached by other surface-attached bacteria.
| S-EPMC3388212 | biostudies-other
Project description:Metastable-state photoacids (mPAHs) are chemical species whose photo-activated state is long-lived enough to allow for proton diffusion. Liao's photoacid (1) represents the archetype of mPAHs, and is being widely used on account of its unique capability to change the acidity of aqueous solutions reversibly. The behavior of 1 in water, however, still remains poorly understood. Herein, we provide in-depth insights on the thermodynamics and kinetics of 1 in water through a series of comparative 1H NMR and UV-Vis studies and relative modelling. Under dark conditions, we quantified a three-component equilibrium system where the dissociation (K a) of the open protonated form (MCH) is followed by isomerization (K c) of the open deprotonated form (MC) to the closed spiropyran form (SP) - i.e., in the absence of light, the ground state acidity can be expressed as K GS a = K a(1 + K c). On the other hand, under powerful and continuous light irradiation we were able to assess, for the first time experimentally, the dissociation constant (K MS a) of the protonated metastable state (cis-MCH). In addition, we found that thermal ring-opening of SP is always rate-determining regardless of pH, whereas hydrolysis is reminiscent of what is found for Schiff bases. The proposed methodology is general, and it was applied to two other compounds bearing a shorter (ethyl, 2) and a longer (butyl, 3) alkyl-1-sulfonate bridge. We found that the pK a remains constant, whereas both pK c and pK MS a linearly increase with the length of the alkyl bridge. Importantly, all results are consistent with a four-component model cycle, which describes perfectly the full dynamics of proton release/uptake of 1-3 in water. The superior hydrolytic stability and water solubility of compound 3, together with its relatively high pK GS a (low K c), allowed us to achieve fully reversible jumps of 2.5 pH units over 18 consecutive cycles (6 hours).
| S-EPMC8163397 | biostudies-literature
Project description:We present a novel technology for microfluidic elastometry and demonstrate its ability to measure stiffness of blood clots as they form. A disposable micro-capillary strip draws small volumes (20 ?L) of whole blood into a chamber containing a surface-mounted micropost array. The posts are magnetically actuated, thereby applying a shear stress to the blood clot. The posts' response to magnetic field changes as the blood clot forms; this response is measured by optical transmission. We show that a quasi-static model correctly predicts the torque applied to the microposts. We experimentally validate the ability of the system to measure clot stiffness by correlating our system with a commercial thromboelastograph. We conclude that actuated surface-attached post (ASAP) technology addresses a clinical need for point-of-care and small-volume elastic haemostatic assays.
| S-EPMC4545258 | biostudies-literature
Project description:Surface-attached micro- and nanobubbles are known for their resistance to external forces. This study experimentally and theoretically investigates their response to strong ultrasonic fields. Surface-attached micro- and nanobubbles with contact radii from 2 μm to 20 μm are generated in a microchannel and exposed to ultrasound through a vibrating glass substrate. At a driving frequency over 200 kHz up to 2 MHz tested, no significant response from the micro- and nanobubbles is observed. By contrast, at 100 kHz-200 kHz, ultrasonic cavitation bubbles appear in the microchannel and migrate toward the surface micro- and nanobubbles. Then the surface micro- and nanobubbles merge with the ultrasonic cavitation bubbles, detach from the substrate, and become free gaseous nuclei susceptible to further cavitation. Notably, the removal process leaves no observable residue. Theoretical analysis suggests that the directional migration of cavitation bubbles is driven by mutual acoustic radiation forces. This work demonstrates that ultrasonic fields can effectively remove surface micro- and nanobubbles, transforming them into free gaseous cavitation nuclei.
| S-EPMC11365372 | biostudies-literature