Adsorption of Lead and Nickel on to Expanded Graphite Decorated with Manganese Oxide Nanoparticles

In this study, expanded graphite (EG) was decorated with manganese oxide nanoparticles (MONPs) by the hydrothermal method, and the newly formed composite (MONPs-EG) was applied as adsorbent for the removal of heavy metals from aqueous solutions. The comparative and competitive adsorption of Pb2+ and Ni2+ (0.01–1.00 mM) on MONPs-EG was investigated. Data from isothermal adsorption of single and binary systems suggested that both Pb2+ and Ni2+ were well described by the Langmuir isotherm, and the maximum adsorption capacities at 298 K were calculated at 0.278 and 0.113 mmol/g for Pb2+ and Ni2+, respectively. In binary systems, a dramatic decrease in adsorption capacity of Ni2+ was observed, while the adsorption capacity of Pb2+ was almost stable, indicating the favorable adsorption of Pb2+ over Ni2+ onto the prepared adsorbent. Kinetics studies of single and binary systems showed that a pseudo-second order model could explain the adsorption processes well. Thermodynamic analysis results demonstrated that the adsorption of these metal ions on the prepared adsorbent is spontaneous and exothermic in nature. The adsorption capacity of MONPs-EG increased significantly in the presence of humic acids. Overall, the results of this study suggest that MONPs-EG can be used effectively as an adsorbent for heavy metals removal from aqueous solutions

The C‑Terminal of Na_V1.7 Is Ubiquitinated by NEDD4L

NaV1.7, the neuronal voltage-gated sodium channel isoform, plays an important role in the human body’s ability to feel pain. Mutations within NaV1.7 have been linked to pain-related syndromes, such as insensitivity to pain. To date, the regulation and internalization mechanisms of the NaV1.7 channel are not well known at a biochemical level. In this study, we perform biochemical and biophysical analyses that establish that the HECT-type E3 ligase, NEDD4L, ubiquitinates the cytoplasmic C-terminal (CT) region of NaV1.7. Through in vitro ubiquitination and mass spectrometry experiments, we identify, for the first time, the lysine residues of NaV1.7 within the CT region that get ubiquitinated. Furthermore, binding studies with an NEDD4L E3 ligase modulator (ubiquitin variant) highlight the dynamic partnership between NEDD4L and NaV1.7. These investigations provide a framework for understanding how NEDD4L-dependent regulation of the channel can influence the NaV1.7 function