The use of organizational assessments in improving patient and staff experiences in the ambulatory care setting

As the needs of patients evolve, healthcare organizations must diversify their approach to improving patient experience. Their programs should encompass the medical, mental, spiritual, and emotional needs of patients and their family members and the staff who care for patients. This case study examines the results of the evaluation to assess the effectiveness of organizational patient experience efforts. The Beryl Institute’s Experience Assessment was the evaluation tool administered and revealed the areas in which the organization was performing well and where improvements were needed. In collaboration with Ambulatory Care and Finance, the Office of Patient Experience targeted the Adult Primary Care and Orthopedic outpatient clinics for this assessment and followed-up with improvement projects to address the areas of opportunities identified. We administered the Extended DiSC® Assessment to the leaders in all departments that function within Ambulatory Care, to support the success of the improvement projects. The DiSC® assessment enables each leader to understand their communication style and gain an understanding of the ways they could improve communication with the leaders they collaborated with, who have different communication styles. Both assessments are geared towards self-examination and prodded the organization towards taking an honest look at how they functioned collectively and on an individual level and helped to clarify their perspective and reiterate their core values as a patient experience organization. The use of the Experience Assessment enabled an objective evaluation of the team’s readiness for patient experience improvements, in conjunction with the insights gleaned from the Extended DiSC® assessment. Experience Framework This article is associated with the Staff & Provider Engagement lens of The Beryl Institute Experience Framework. (http://bit.ly/ExperienceFramework) Access other PXJ articles related to this lens. Access other resources related to this lens

Enzymatic and Bioinspired Systems for Hydrogen Production

The extraordinary potential of hydrogen as a clean and sustainable fuel has sparked the interest of the scientific community to find environmentally friendly methods for its production. Biological catalysts are the most attractive solution, as they usually operate under mild conditions and do not produce carbon-containing byproducts. Hydrogenases promote reversible proton reduction to hydrogen in a variety of anoxic bacteria and algae, displaying unparallel catalytic performances. Attempts to use these sophisticated enzymes in scalable hydrogen production have been hampered by limitations associated with their production and stability. Inspired by nature, significant efforts have been made in the development of artificial systems able to promote the hydrogen evolution reaction, via either electrochemical or light-driven catalysis. Starting from small-molecule coordination compounds, peptide- and protein-based architectures have been constructed around the catalytic center with the aim of reproducing hydrogenase function into robust, efficient, and cost-effective catalysts. In this review, we first provide an overview of the structural and functional properties of hydrogenases, along with their integration in devices for hydrogen and energy production. Then, we describe the most recent advances in the development of homogeneous hydrogen evolution catalysts envisioned to mimic hydrogenases

Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster

De novo design provides an attractive approach, which allows one to test and refine the principles guiding metalloproteins in defining the geometry and reactivity of their metal ion cofactors. Although impressive progress has been made in designing proteins that bind transition metal ions including iron–sulfur clusters, the design of tetranuclear clusters with oxygen‐rich environments remains in its infancy. In previous work, we described the design of homotetrameric four‐helix bundles that bind tetra‐Zn2+ clusters. The crystal structures of the helical proteins were in good agreement with the overall design, and the metal‐binding and conformational properties of the helical bundles in solution were consistent with the crystal structures. However, the corresponding apo‐proteins were not fully folded in solution. In this work, we design three peptides, based on the crystal structure of the original bundles. One of the peptides forms tetramers in aqueous solution in the absence of metal ions as assessed by CD and NMR. It also binds Zn2+ in the intended stoichiometry. These studies strongly suggest that the desired structure has been achieved in the apo state, providing evidence that the peptide is able to actively impart the designed geometry to the metal cluster

A group-theoretic approach to the origin of chirality-induced spin selectivity in non-magnetic molecular junctions

Spin-orbit coupling gives rise to a range of spin-charge interconversion phenomena in non-magnetic systems where spatial symmetries are reduced or absent. Chirality-induced spin selectivity (CISS), a term that generically refers to a spin-dependent electron transfer in non-magnetic chiral systems, is one such case, appearing in a variety of seemingly unrelated situations ranging from inorganic materials to molecular devices. In particular, the origin of CISS in molecular junctions is a matter of an intense current debate. Here we contend that the necessary conditions for the CISS effect to appear can be generally and fully understood on the basis of a complete symmetry analysis of the molecular junction, and not only of the molecule. Our approach, which draws on the use of point-group symmetries within the scattering formalism for transport, shows that electrode symmetries are as important as those of the molecule when it comes to the emergence of a spin-polarization and, therefore, a possible appearance of CISS. It turns out that standalone metallic nanocontacts can exhibit spin-polarization when relative rotations are introduced which reduce the symmetry. As a corollary, molecular junctions with $\textbf{achiral}$ molecules can also exhibit spin polarization along the direction of transport, provided that the whole junction is chiral. This formalism also allows to predict the qualitative changes on the spin-polarization upon substitution of a chiral molecule in the junction with its enantiomeric partner. Quantum transport calculations based on density functional theory corroborate all of our predictions and provide further quantitative insight.Comment: 19 pages, 4 figures, 1 tabl

High-level HIV-1 Nef transient expression in Nicotiana benthamiana using the P19 gene silencing suppressor protein of Artichoke Mottled Crinckle Virus

<p>Abstract</p> <p>Background</p> <p>In recent years, different HIV antigens have been successfully expressed in plants by either stable transformation or transient expression systems. Among HIV proteins, Nef is considered a promising target for the formulation of a multi-component vaccine due to its implication in the first steps of viral infection. Attempts to express Nef as a single protein product (not fused to a stabilizing protein) in transgenic plants resulted in disappointingly low yields (about 0.5% of total soluble protein). In this work we describe a transient expression system based on co-agroinfiltration of plant virus gene silencing suppressor proteins in <it>Nicotiana benthamiana</it>, followed by a two-step affinity purification protocol of plant-derived Nef.</p> <p>Results</p> <p>The effect of three gene silencing viral suppressor proteins (P25 of Potato Virus X, P19 of either Artichoke Mottled Crinckle virus and Tomato Bushy Stunt virus) on Nef transient expression yield was evaluated. The P19 protein of Artichoke Mottled Crinckle virus (AMCV-P19) gave the highest expression yield in vacuum co-agroinfiltration experiments reaching 1.3% of total soluble protein, a level almost three times higher than that previously reported in stable transgenic plants. The high yield observed in the co-agroinfiltrated plants was correlated to a remarkable decrease of Nef-specific small interfering RNAs (siRNAs) indicating an effective modulation of RNA silencing mechanisms by AMCV-P19. Interestingly, we also showed that expression levels in top leaves of vacuum co-agroinfiltrated plants were noticeably reduced compared to bottom leaves. Moreover, purification of Nef from agroinfiltrated tissue was achieved by a two-step immobilized metal ion affinity chromatography protocol with yields of 250 ng/g of fresh tissue.</p> <p>Conclusion</p> <p>We demonstrated that expression level of HIV-1 Nef in plant can be improved using a transient expression system enhanced by the AMCV-P19 gene silencing suppressor protein. Moreover, plant-derived Nef was purified, with enhanced yield, exploiting a two-step purification protocol. These results represent a first step towards the development of a plant-derived HIV vaccine.</p

Synthesis of temporin L hydroxamate-based peptides and evaluation of their coordination properties with iron (III)

Ferric iron is an essential nutrient for bacterial growth. Pathogenic bacteria synthesize iron-chelating entities known as siderophores to sequestrate ferric iron from host organisms in order to colonize and replicate. The development of antimicrobial peptides (AMPs) conjugated to iron chelators represents a promising strategy for reducing iron availability, inducing bacterial death, and enhancing simultaneously the efficacy of AMPs. Here we designed, synthesized, and characterized three hydroxamate-based peptides Pep-cyc1, Pep-cyc2, and Pep-cyc3, derived from a cyclic temporin L peptide (Pep-cyc) developed previously by some of us. The Fe3+ complex formation of each ligand was characterized by UVvisible spectroscopy, mass spectrometry, IR, and NMR spectroscopies. In addition, the effect of Fe3+ on the stabilization of -helix conformation of hydroxamate-based peptides and the cotton effect were examined by CD spectroscopy. Moreover, the antimicrobial results obtained in vitro on some Gram-negative strains (K. Pneumoniae and E. coli) showed the ability of each peptide to chelate efficaciously Fe3+ obtaining a reduction of MIC values in comparison to their parent peptide Pepcyc. Our results demonstrated that siderophore conjugation could increase the efficacy and selectivity of AMPs used for the treatment of infectious diseases caused by Gram-negative pathogens

A biomimetic metalloporphyrin catalyzes indole oxidation with high selectivity

Indole is one of the most common heterocyclic scaffolds available in nature. It occurs in several natural compounds, including alkaloids, plant hormones, flower scents and dyes.1 Despite the structural simplicity of this molecule, indole oxidation commonly results in the formation of a large number of products, including the 2- or 3-oxygenated compounds, di-oxygenated and more complex molecules. For this reason, indole oxidation has become a widespread model reaction to test the efficacy of both biological catalysts2,3 and their synthetic analogues.4,5 Most of the catalysts examined so far gave poor selectivity toward any of the oxidation products.2-5 Here we present the results concerning oxidation of indole and its derivatives catalyzed by Mn-Mimochrome VI*a (Mn-MC6*a). Mn-MC6*a is a synthetic peptide-porphyrin conjugate conceived to act as a miniaturized heme-protein model.6 Mn-MC6*a is able to oxidize indole under unprecedented site-selective conditions, yielding to 3-oxindolenine as single product. Additionally, the reaction selectivity is dramatically altered when 1- or 3-methyl-substituted indoles are used as substrates. The formation and isolation of the reactive 3-oxindolenine is highly important, since it is believed to represent a useful synthon in organic synthesis. Accordingly, the exploitation of its reactivity with nucleophiles, in order to provide one pot transformations, is currently ongoing, with the aim to further increase the synthetic potential of our catalyst. 1. Burton, T.C. in Heterocyclic scaffolds II: Reactions and applications of indoles; Gribble, G.W., Ed.; Springer-Verlag Berlin Heidelberg, 2011. 2. Kuo, H. H. and Mauk, A. G.; Proc. Natl. Acad. Sci. U. S. A. 2012, 109, 13966–13971. 3. Barrios, D. A. et al. J. Am. Chem. Soc. 2014, 136, 7914-7925. 4. Linhares, M. et al. Appl. Catal. A. 2014, 470, 427–433. 5. Poon L. C.-H. et al. J. Am. Chem. Soc. 2011, 133, 1877–1884. 6. Caserta, G. et al. ChemBioChem 2018 (doi: 10.1002/cbic.201800200