Scribes with PGY-1 Residents on Inpatient Medicine Teams: Effect on Time Spent in Meaningful Work.

Background: The high documentation demands and limited time in direct patient care in the first year of internal medicine residency represent concerns for burnout and low job satisfaction in this important year of training. Objective: To assess the effect of scribes on the time PGY-1 residents spent on various work tasks. Methods: Participants were 24 PGY-1 internal medicine residents on two inpatient medicine teams at one site for 6 months (September 2019-February 2020). Residents were assigned a scribe during the first or second 2 weeks of a 4-week rotation and had no scribe for the other 2 weeks. Time study observers documented resident work activities. Residents ranked the meaningfulness of work activities via survey at the end of each 2-week period. Results: Of 24 residents, 18 (75%) completed the survey at both time points. Residents ranked patient care as the most meaningful and EHR work as the least meaningful work activity. EHR work claimed the largest percentage of time, with or without a scribe (mean, 33.2% and 39%, respectively). With a scribe, residents spent significantly less time (-5.8%, P < 0.0001) in EHR work and significantly more time (1.3%, P = 0.0267) in direct patient care and coordinating patient care (3.0%, P < 0.0001). Conclusions: The presence of a scribe with PGY-1 internal medicine residents on inpatient teams resulted in a significantly greater percentage of total work time spent in work they considered most meaningful and a significantly lower percentage of total work time in work they considered least meaningful.

Interactions of amyloid Aß(1-42) peptide with self-assembled peptide nanospheres.

In this work we have probed the interactions of the amyloid Aß(1-42) peptide with self-assembled nanospheres. The nanospheres were formed by self-assembly of a newly developed bolaamphiphile bis(N-alpha-amido-methionine)-1,8 octane dicarboxylate under aqueous conditions. It was found that the interactions of the Aß(1-42) peptide with the nanospheres were concentration as well as pH dependent and the peptide largely adopts a random coil structure upon interacting with the nanospheres. Further, upon incorporation with the nanospheres, we observed a relative diminution in the aggregation of Aß(1-42) at low concentrations of Aß(1-42). The interactions between the nanospheres and the Aß(1-42) peptide were investigated by atomic force microscopy, transmission electron microscopy, circular dichroism, FTIR and fluorescence spectroscopy, and the degree of fibrillation in the presence and absence of nanospheres was monitored by the Thioflavine T assay. We believe that the outcome from this work will help further elucidate the binding properties of Aß peptide as well as designing nanostructures as templates for further investigating the nucleation and fibrillation process of Aß-like peptides.

Urea facilitates the translocation of single-stranded DNA and RNA through the alpha-hemolysin nanopore.

The staphylococcal alpha-hemolysin (alphaHL) protein nanopore is under investigation as a fast, cheap detector for nucleic acid analysis and sequencing. Although discrimination of all four bases of DNA by the alphaHL pore has been demonstrated, analysis of single-stranded DNAs and RNAs containing secondary structure mediated by basepairing is prevented because these nucleic acids cannot be translocated through the pore. Here, we show that a structured 95-nucleotide single-stranded DNA and its RNA equivalent are translocated through the alphaHL pore in the presence of 4 M urea, a concentration that denatures the secondary structure of the polynucleotides. The alphaHL pore is functional even in 7 M urea, and therefore it is easily stable enough for analyses of challenging DNA and RNA species.

DNA strands from denatured duplexes are translocated through engineered protein nanopores at alkaline pH.

Nanopores are under development for the detection of a variety of analytes and the investigation of chemical reactions at the single molecule level. In particular, the analysis of nucleic acid molecules is under intense investigation, including the development of systems for rapid, low-cost DNA sequencing. Here, we show that DNA can be translocated through an engineered alphaHL protein pore at pH 11.7, a value at which dsDNA is denatured. Therefore, the alphaHL pore is sufficiently stable to entertain the possibility of direct nanopore sequencing of genomic dsDNA samples, which are more readily obtained and handled than ssDNA.

Morphology controlled growth of chitosan-bound microtubes and a study of their biocompatibility and antibacterial activity.

Self-assembled peptide microtubes are fabricated with the biopolymer chitosan. The microtubes are covalently attached to chitosan and the morphology of the chitosan assembled on the surface of the microtubes can be tuned by altering the pH of the growth solution. Cytotoxicity studies in the presence of mouse embryonic fibroblasts indicate that the chitosan-bound microtubes are highly biocompatible and the cells are able to survive and proliferate at a similar rate to the control. Antibacterial studies in the presence of E. coli prove that the chitosan-bound microtubes are bactericidal. This simple method for the development of biocompatible microstructures will facilitate cell targeting, fabrication of efficient carrier devices, and the preparation of highly efficient antibacterial materials.

Investigation of insulin loaded self-assembled microtubules for drug release.

Self-assembled microtubules were used to entrap insulin for the preparation of new drug delivery devices. The interactions of insulin with the microtubules were probed by circular dichroism, zeta potential analysis, as well as FTIR spectroscopy. The morphologies of the insulin-loaded tubules were examined by AFM and TEM. We found that insulin loading was both pH- as well as concentration-dependent. The circular dichroism analysis indicated that, at pH range 6-7, the conformation change in the presence of the microtubules was minimal and hence would be the most appropriate conditions for insulin loading. The entrapment efficiency and release of insulin was found to be pH-dependent. Further, the controlled drug release studies indicated that, under acidic conditions, insulin release was extremely slow, and it is likely that the insulin is protected inside the microtubules. Thus, the microtubules may potentially protect the insulin from aggregation and release at lower pH (gastric pH) in ViVo. However, at pH 6.5 (closer to intestinal pH) a sustained release was observed. Such new materials may inhibit the aggregation of peptides under suitable conditions and potentially be used for drug delivery, in particular, for other peptide-based drugs.