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1.
Adv Neonatal Care ; 21(3): 189-197, 2021 Jun 01.
Article in English | MEDLINE | ID: mdl-33009153

ABSTRACT

BACKGROUND: Diaper dermatitis (DD) causes discomfort and emotional distress and creates possible sources of infection among newborn intensive care unit infants. Diaper dermatitis remains prevalent despite studies documenting an understanding of prevention and treatment modalities. Standardizing perineal skin care guidelines could reduce DD. PURPOSE: Implement perineal skin care guidelines, while introducing novel diaper wipes, to decrease the incidence of DD by 20% within a 1-year period. METHODS: Our unit reviewed evidence-based literature to develop a standardized perineal care guideline for prevention and treatment, encompassing the use of novel, preservative-free diaper wipes with grapefruit seed extract. The outcome measures were the incidence and duration of DD. Process compliances were monitored. The balancing measure was the rate of fungal skin infection while using preservative-free wipes. FINDINGS: Between July 2017 and March 2019, 1070 infants were admitted for 1 or more days, with 11% of those being born at less than 30 weeks of gestational age. After guideline implementation in January 2018, the incidence of DD decreased by 16.7%. The incidence of severe cases dropped by 34.9%, with 3.5 days per 100 patient-days shortened duration. Process compliance was achieved. Neonates tolerated the novel wipes without increased fungal skin infection. IMPLICATIONS FOR PRACTICE: The Perineal Skin Care Guidelines could reduce the rate and duration of DD. Newborn intensive care unit infants tolerated the novel diaper wipes. IMPLICATIONS FOR RESEARCH: Additional research on wipes containing other types of extracts or ingredients.


Subject(s)
Diaper Rash , Intensive Care Units, Neonatal , Child , Diaper Rash/prevention & control , Humans , Infant , Infant Care , Infant, Newborn , Quality Improvement , Skin Care
2.
Biol Chem ; 387(4): 477-83, 2006 Apr.
Article in English | MEDLINE | ID: mdl-16606347

ABSTRACT

The fusion-active conformation of the envelope protein gp41 of HIV-1 consists of an N-terminal trimeric alpha-helical coiled-coil domain and three anti-parallel C-terminal helices that fold down the grooves of the coiled-coil to form a six-helix bundle. Disruption of the six-helix bundle is considered to be a key component of an effective non-peptide fusion inhibitor. In the current study, a fluorescence resonance energy transfer (FRET) experiment for the detection of inhibitor binding to the gp41 N-peptide coiled-coil of HIV-1 was performed, utilizing peptide inhibitors derived from the gp41 C-terminal helical region. The FRET acceptor is a 31-residue N-peptide containing a known deep hydrophobic pocket, stabilized into a trimer by ferrous ion ligation. The FRET donor is a 16-18-residue fluorophore-labeled C-peptide, designed to test the specificity of the N-C interaction. Low microM dissociation constants were observed, correlated to the correct sequence and helical propensity of the C-peptides. Competitive inhibition was demonstrated using the assay, allowing for rank ordering of peptide inhibitors according to their affinity in the 1-20 microM range. The assay was conducted by measuring fluorescence intensity in 384-well plates. The rapid detection of inhibitor binding may permit identification of novel drug classes from a library.


Subject(s)
Fluorescence Resonance Energy Transfer/methods , HIV Envelope Protein gp41/analysis , Amino Acid Sequence , Anti-HIV Agents/chemistry , Anti-HIV Agents/metabolism , Anti-HIV Agents/pharmacology , HIV Envelope Protein gp41/chemistry , HIV Envelope Protein gp41/metabolism , Hydrophobic and Hydrophilic Interactions , Ligands , Molecular Sequence Data , Peptides/chemistry , Peptides/metabolism , Peptides/pharmacology , Protein Binding , Protein Conformation , Sequence Analysis, Protein
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