The tailored synthesis of homo (A2) and hetero (AB) N-substituted peri-xanthenoxanthene diimides (PXXDIs) and peri-functionalized PXX monoimides (PXXMIs) from 3-hydroxy naphthalic anhydride is described. As A2-type PXXDIs could be synthesized in one step, AB-type PXXDIs and PXXMIs were prepared through a modular approach capitalizing on sequential Suzuki coupling, Imidation and Pummerer reactions with very high yields. In view of their potential applications as organic semiconductors, self-organization studies were performed through liquid deposition on surfaces, depicting the formation of islands, needles and rods.
Lysine acetylation is a prevalent post-translational modification in both eukaryotes and prokaryotes. Whereas this modification is known to play pivotal roles in eukaryotes, the function and extent of this modification in prokaryotic cells remain largely unexplored. Here we report the acetylome of a pair of antibiotic-sensitive and -resistant nosocomial pathogen Acinetobacter baumannii SK17-S and SK17-R. A total of 145 lysine acetylation sites on 125 proteins was identified, and there are 23 acetylated proteins found in both strains, including histone-like protein HU which was found to be acetylated at Lys13. HU is a dimeric DNA-binding protein critical for maintaining chromosomal architecture and other DNA-dependent functions. To analyze the effects of site-specific acetylation, homogenously Lys13-acetylated HU protein, HU(K13ac) was prepared by genetic code expansion. Whilst not exerting an obvious effect on the oligomeric state, Lys13 acetylation alters both the thermal stability and DNA binding kinetics of HU. Accordingly, this modification likely destabilizes the chromosome structure and regulates bacterial gene transcription. This work indicates that acetyllysine plays an important role in bacterial epigenetics.
Dioxygen adsorbs in the end-on configuration on-top of the Fe atoms of an iron phthalocyanine monolayer supported on Ag(100) and is partly cleaved at room temperature to produce O/FePc/Ag(100). Scanning tunnelling microscopy coupled to density functional theory calculations gives the first experimental evidence of the substrate involvement in the O2 bond dissociation.
We report on the assembly of a highly ordered array of copper tetrameric clusters, coordinated into a metal-organic network. The ordered cluster array has been achieved by the deposition of tetrahydroxyquinone molecules on the Cu(111) surface at room temperature, and subsequent thermally activated dehydrogenation with the formation of tetraoxyquinone tetra-anions with a 4 × 4 periodicity. The supramolecular organic network acts as a spacer for the highly ordered two-dimensional network of copper tetramers at the very surface.
Extracellular matrix (ECM)-mimicking surfaces are pivotal tools in understanding adherent cell physiopathology. In this sense, we have recently reported on a discrete set of ECM-mimicking SAMs, among which only those exposing IGDQ peptide-alkanethiols sustain the adhesion of MDA-MB-231 cells by triggering FAK phosphorylation and peculiarly induce the migration of individual cancer cells on the subcentimeter scale. Starting from the experimentally observed relationship among the SAM composition, organization, and biological response, a systematic computational characterization aided in pinpointing the atomistic details through which specific composition and organization achieve the desired biological responsiveness. Specifically, the solvent, number and type of peptides, and presence or absence of surface fillers were accurately considered, creating representative model SAMs simulated by means of classical molecular dynamics (MD) with a view toward unravelling the experimental evidence, revealing how the conformational and structural features of these substrates dictate the specific motogenic responses. Through complementary experimental and computational investigations, it clearly emerges that there exists a distinct and precise mutual interaction among IGDQ-peptides, the surface fillers, and Au, which controls the structural properties of the ECM-mimicking SAMs and thus their motogenic potential.
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