Functionalization of Polymer-Wrapped Silver Nanoclusters and Potential Applications as Antimicrobial Mask Materials.

The poly(methacrylic acid) (PMAA) polymer stabilized silver nanoclusters Ag ( = 2-9), synthesized in aqueous solution by the selected light wavelength irradiation photolysis approach, have been functionalized with thiol and amine ligands and successfully transferred from aqueous to organic media. Low- or high-resolution positive mass spectra showed constant species composites with the molecular formula AgL [ = 2 to ∼9, L = butylmercaptan (CHS), thiolphenol (CHS), or dodecanethiol (CHS)] and proved that the molecules consist of deprotonated sulfur ligands in each species with one positive charge. Fourier transform infrared and X-ray photoelectron spectroscopy are consistent, indicating deprotonated sulfur, while silver has a zero valence value.

The Role of Phosphorylation and Acylation in the Regulation of Drug Resistance in .

Tuberculosis is a chronic and lethal infectious disease caused by . In previous decades, most studies in this area focused on the pathogenesis and drug targets for disease treatments. However, the emergence of drug-resistant strains has increased the difficulty of clinical trials over time.

Mdivi-1, a mitochondrial fission inhibitor, modulates T helper cells and suppresses the development of experimental autoimmune encephalomyelitis.

Background: Unrestrained activation of Th1 and Th17 cells is associated with the pathogenesis of multiple sclerosis and its animal model, experimental autoimmune encephalomyelitis (EAE). While inactivation of dynamin-related protein 1 (Drp1), a GTPase that regulates mitochondrial fission, can reduce EAE severity by protecting myelin from demyelination, its effect on immune responses in EAE has not yet been studied.

Methods: We investigated the effect of Mdivi-1, a small molecule inhibitor of Drp1, on EAE.

Lysine acetylation regulates the activity of Escherichia coli pyridoxine 5'-phosphate oxidase.

Nɛ-lysine acetylation is one of the most abundant post-translational modifications in eukaryote and prokaryote. Protein acetylome of Escherichia coli has been screened using mass spectrometry (MS) technology, and many acetylated proteins have been identified, including the pyridoxine 5'-phosphate oxidase (EcPNPOx), but the biological roles played by lysine acetylation in EcPNPOx still remain unknown. In this study, EcPNPOx was firstly overexpressed and purified, and two acetylated lysine residues were identified by the subsequent liquid chromatography-tandem mass spectrometry analysis.

Lysine acetylation regulates the activity of Escherichia coli S-adenosylmethionine synthase.

Lysine acetylation is one of the most abundant post-translational modifications. However, physiological roles of this modification in bacteria are largely unknown. Previous protein acetylome analysis showed that Escherichia coli adenosylmethionine synthase (MAT) undergoes acetylation in vivo, but the biological functions of this modification still need to be uncovered.