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Abstract: Core/shell nanocrystals with a graded interface between core and shell exhibit improved optoelectronic properties compared with particles with an abrupt, sharp interface. Material gradients mitigate interfacial defects and define the shape of the confinement potential. So far, few works exist that allow to quantify the width of the gradient. In this study, ZnSe/CdS nanocrystals with graded shells made at different temperatures are characterized using extended X-ray absorption fine structure (EXAFS) and Raman spectroscopies. The average coordination number of the probed element with respect to the two possible counterions is fit to a simple, geometric model. It is shown that at the lower temperature limit for shell growth (260 °C), substantial interfacial alloying can be attributed mainly to cation migration. At higher temperature (290 °C), strain minimization leads to atomic ordering of the metal ions and an anomalously low degree of phase mixing.

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Abstract: The construction and manipulation of amine-containing architectures is of importance to academic and industrial development and discovery programs. The photochemical single-electron reduction of imine derivatives to generate α-amino radical intermediates has emerged as a powerful umpolung strategy for opening up underexplored routes to such amine motifs. Furthermore, these radicals have been shown to engage in a wide variety of chemistry, including radical–radical coupling, addition to electrophiles, and reductive amination chemistry. The concept has also begun to see application to iminium ion intermediates and the extension to enantiocontrolled C–C bond formation. This Perspective covers recent efforts in this synthetic strategy to simple and complex amine structures alike.

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Abstract: The self-assembly behaviour and antimicrobial activity of two new designed amphiphilic peptides, R3F3 and R4F4, containing short hydrophobic phenylalanine (F) cationic arginine (R) sequences are investigated. The conformation of the peptides was examined using circular dichroism and FTIR spectroscopy, which show that they have a disordered secondary structure. Concentration-dependent fluorescence assays show the presence of a critical aggregation concentration (cac) for each peptide. Above the cac, small angle x-ray scattering (SAXS) and transmission electron microscopy (TEM) show the presence of a population of twisted tapes for R3F3 and nanosheets for R4F4. The interaction of the peptides with model bacterial membranes comprising mixtures of the lipids DPPG [1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol)] and DPPE [1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine], was studied using SAXS and cryogenic-TEM. Analysis of the SAXS structure factor indicates that R3F3 interacts with lipid bilayers by inducing correlation between bilayers, whereas R4F4 interacts with the bilayers causing an increase in polydispersity of the vesicle wall thickness. Both peptides break vesicles with a 1:3 DPPG:DPPE composition, which is close to the ratio of PG and PE lipids observed in the lipid membrane of Pseudomonas aeruginosa, a pathogen responsible for serious infections and which has developed antimicrobial resistant strains. Both peptides show activity against this bacterium in planktonic form. Peptide R4F4 shows particularly strong bioactivity against this microbe, with a minimum inhibitory concentration (MIC) value in the range of concentrations where the peptide is cytocompatible. It was further shown to have activity against other Pseudomonas species including the common plant pathogen P. syringae. Finally, we show that R4F4 inhibits the development of P. aeruginosa biofilms. This was examined in detail and a proposed mechanism involving binding of the signalling molecule c-di-GMP is suggested, based on circular dichroism spectroscopy studies and Congo red assays of extracellular polysaccharides produced by the stressed bacteria. Thus, R4F4 is a promising candidate antimicrobial peptide with activity against Pseudomonas species.

Open Access

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Abstract: With the increasing trend of using microcrystals and intense microbeams at synchrotron X-ray beamlines, radiation damage becomes a more pressing problem. Theoretical calculations show that the photoelectrons that primarily cause damage can escape microcrystals. This effect would become more pronounced with decreasing crystal size as well as at higher energies. To prove this effect, data from cryocooled lysozyme crystals of dimensions 5 × 3 × 3 and 20 × 8 × 8 µm mounted on cryo-transmission electron microscopy (cryo-TEM) grids were collected at 13.5 and 20.1 keV using a PILATUS CdTe 2M detector, which has a similar quantum efficiency at both energies. Accurate absorbed doses were calculated through the direct measurement of individual crystal sizes using scanning electron microscopy after the experiment and characterization of the X-ray microbeam. The crystal lifetime was then quantified based on the D1/2 metric. In this first systematic study, a longer crystal lifetime for smaller crystals was observed and crystal lifetime increased at higher X-ray energies, supporting the theoretical predictions of photoelectron escape. The use of detector technologies specifically optimized for data collection at energies above 20 keV allows the theoretically predicted photoelectron escape to be quantified and exploited, guiding future beamline-design choices.

Open Access

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Abstract: Long non-coding RNAs (lncRNAs) constitute a significant fraction of the transcriptome, playing important roles in development and disease. However, our understanding of structure-function relationships for this emerging class of RNAs has been limited to secondary structures. Here, we report the 3-D atomistic structural study of epigenetic lncRNA, Braveheart (Bvht), and its complex with CNBP (Cellular Nucleic acid Binding Protein). Using small angle X-ray scattering (SAXS), we elucidate the ensemble of Bvht RNA conformations in solution, revealing that Bvht lncRNA has a well-defined, albeit flexible 3-D structure that is remodeled upon CNBP binding. Our study suggests that CNBP binding requires multiple domains of Bvht and the RHT/AGIL RNA motif. We show that RHT/AGIL, previously shown to interact with CNBP, contains a highly flexible loop surrounded by more ordered helices. As one of the largest RNA-only 3-D studies, the work lays the foundation for future structural studies of lncRNA-protein complexes.