In order to better understand the physical basis of the biological activity of nanoparticles (NPs) in nanomedicine applications and under conditions of environmental exposure, we performed an array of photophysical measurements to quantify the interaction of model gold NPs having a wide range of NP diameters with common blood proteins. In particular, absorbance, fluorescence quenching, circular dichroism, dynamic light scattering, and electron microscopy measurements were performed on surface-functionalized water-soluble gold NPs having a diameter range from 5 to 100 nm in the presence of common human blood proteins: albumin, fibrinogen, gamma-globulin, histone, and insulin. We find that the gold NPs strongly associate with these essential blood proteins where the binding constant, K, as well as the degree of cooperativity of particle--protein binding (Hill constant, n), depends on particle size and the native protein structure. We also find tentative evidence that the model proteins undergo conformational change upon association with the NPs and that the thickness of the adsorbed protein layer (bare NP diameter <50 nm) progressively increases with NP size, effects that have potential general importance for understanding NP aggregation in biological media and the interaction of NP with biological materials broadly.
Because of their outstanding electrical and mechanical properties, graphene strain sensors have attracted extensive attention for electronic applications in virtual reality, robotics, medical diagnostics, and healthcare. Although several strain sensors based on graphene have been reported, the stretchability and sensitivity of these sensors remain limited, and also there is a pressing need to develop a practical fabrication process. This paper reports the fabrication and characterization of new types of graphene strain sensors based on stretchable yarns. Highly stretchable, sensitive, and wearable sensors are realized by a layer-by-layer assembly method that is simple, low-cost, scalable, and solution-processable. Because of the yarn structures, these sensors exhibit high stretchability (up to 150%) and versatility, and can detect both large- and small-scale human motions. For this study, wearable electronics are fabricated with implanted sensors that can monitor diverse human motions, including joint movement, phonation, swallowing, and breathing.
The human cytomegalovirus (HCMV) 72-kDa immediate-early 1 (IE1) protein is thought to modulate cellular antiviral functions impacting on promyelocytic leukemia (PML) nuclear bodies and signal transducer and activator of transcription (STAT) signaling. IE1 consists of four distinct regions: an amino-terminal region required for nuclear localization, a large central hydrophobic region responsible for PML targeting and transactivation activity, an acidic domain, and a carboxyl-terminal chromatin tethering domain. We found that the acidic domain of IE1 is required for binding to STAT2. A mutant HCMV encoding IE1(⌬421-475) with the acidic domain deleted was generated. In mutant virus-infected cells, IE1(⌬421-475) failed to bind to STAT2. The growth of mutant virus was only slightly delayed at a high multiplicity of infection (MOI) but was severely impaired at a low MOI with low-level accumulation of viral proteins. When cells were pretreated with beta interferon, the mutant virus showed an additional 1,000-fold reduction in viral growth, even at a high MOI, compared to the wild type. The inhibition of STAT2 loading on the target promoter upon infection was markedly reduced with mutant virus. Furthermore, sumoylation of IE1 at this acidic domain was found to abolish the activity of IE1 to bind to STAT2 and repress the interferon-stimulated genes. Our results provide genetic evidence that IE1 binding to STAT2 requires the 55-amino-acid acidic domain and promotes viral growth by interfering with interferon signaling and demonstrate that this viral activity is negatively regulated by a cellular sumoylation pathway.
Conjugated polymers possessing polar functionalities were shown to effectively anchor single-walled carbon nanotubes (SWNTs) to the surface of high-capacity anode materials and enable the formation of electrical networks. Specifically, poly[3-(potassium-4-butanoate) thiophene] (PPBT) served as a bridge between SWNT networks and various anode materials, including monodispersed FeO spheres (sFeO) and silicon nanoparticles (Si NPs). The PPBT π-conjugated backbone and carboxylate (COO-) substituted alkyl side chains, respectively, attracted the SWNT π-electron surface and chemically interacted with active material surface hydroxyl (-OH) species to form a carboxylate bond. Beneficially, this architecture effectively captured cracked/pulverized particles that typically form as a result of repeated active material volume changes that occur during charging and discharging. Thus, changes in electrode thickness were suppressed substantially, stable SEI layers were formed, electrode resistance was reduced, and enhanced electrode kinetics was observed. Together, these factors led to excellent electrochemical performance.
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