Improving Discharge Safety in a Pediatric Emergency Department.

BACKGROUND AND OBJECTIVES: Discharge from the emergency department (ED) involves a complex series of steps to ensure a safe transition to home and follow-up care. Preventable, discharge-related serious safety events (SSEs) in our ED highlighted local vulnerabilities. We aimed to improve ED discharge by implementing a standardized discharge process with emphasis on multidisciplinary communication and family engagement. METHODS: At a tertiary children's hospital, we used the model for improvement to revise discharge care. Interventions included a new discharge checklist, a provider huddle emphasizing discharge vital signs, and a scripted discharge review of instructions with families. We used statistical process control to evaluate performance. Primary outcomes included elimination of preventable, discharge-related SSEs and Press Ganey survey results assessing caregiver information for care of child at home. A secondary outcome was number of days between preventable low-level (near-miss, no or minimal harm) events. Process measures included discharge checklist adoption and vital sign acquisition. Balancing measures were length of stay (LOS) and return rates. RESULTS: Over the study period, there were no preventable SSEs and low-level event frequency improved to a peak of >150 days between events. Press Ganey responses regarding quality of discharge information did not change (62%). Checklist use was rapidly adopted, reaching 94%. Vital sign acquisition increased from 67% to 83%. There was no change in the balancing measures of median LOS or return visit rates. CONCLUSIONS: The development and implementation of a standardized discharge process led to the elimination of reported discharge-related events, without increasing LOS or return visits.

Factors contributing to the potency of antimicrobial cationic peptides from the N-terminal region of human lactoferrin.

This study investigated the antimicrobial activities of peptides derived from the N-terminal region of human lactoferrin, and examined the contributions of individual residues to the activity of the most potent peptide. Two regions of antimicrobial activity were identified, the first corresponding to a weakly active peptide, HLP-9, comprising residues 1-9, and a second corresponding to a more potent peptide, HLP-10, comprising residues 18-26 and containing the hexapeptide motif, FQWQRN. Inhibitory studies on peptides from the first region confirm the importance of tryptophan residues in enhancing and broadening peptide activity. Inhibitory studies with glycine-substituted homologues of the more potent peptide showed that F21/G and R25/G substitutions resulted in a major reduction or complete loss of activity, while increased peptide cationicity or flexibility had little effect. Our findings demonstrate that F21 and R25 are critical determinants of potency for HLP-10, and that the second aromatic residue may act synergistically with W23 in developing and enhancing the activity of this cationic peptide.

Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity.

Synthetic peptides derived from human and bovine lactoferricin, as well as tritrpticin sequences, were assayed for antimicrobial activity against wild-type Escherichia coli and LPS mutant strains. Antimicrobial activity was only obtained with peptides derived from the bovine lactoferricin sequence and peptides corresponding to chimeras of human and bovine sequences. None of the peptides corresponding to different regions of native human lactoferricin showed any antimicrobial activity. The results underline the importance of the content of tryptophan and arginine residues, and the relative location of these residues for antimicrobial activity. Results obtained for the same assays performed with LPS mutants suggest that lipid A is not the main binding site for lactoferricin which interacts first with the negative charges present in the inner core. Computer modelling of the most active peptides led to a model in which positively charged residues of the cationic peptide interact with negative charges carried by the LPS to disorganise the structure of the outer membrane and facilitate the approach of tryptophan residues to the lipid A in order to promote hydrophobic interactions.