Evidence map›Paper›PMID 34686153›Full record

ArticleBMC pulmonary medicine2021

Structural and functional stability of the sulfur-free surfactant protein B peptide mimic B-YL in synthetic surfactant lipids.

Frans J Walther, Shantanu Sharma, Larry M Gordon, Alan J Waring

Open access · goldAbstract read
In one paragraph

Article in BMC pulmonary medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Moving on from clinical animal-derived surfactants to peptide-based synthetic pulmonary surfactant.American journal of physiology. Lung cellular and molecular physiology · 2024
    Review
  2. What is new in synthetic lung surfactant protein technology?Expert review of respiratory medicine · 2024
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Frans J WaltherDepartment of Pediatrics, David Geffen School of Medicine, University of California Los Angeles, 405 Hilgard Avenue, Los Angeles, CA, 90095, USA. fjwalther@ucla.edu.
Shantanu SharmaMaterials and Process Simulation Center, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA, 91125, USA.
Larry M GordonLundquist Institute for Biomedical Innovation at Harbor-UCLA Medical Center, 1124 West Carson Street, Torrance, CA, 90502, USA.
Alan J WaringLundquist Institute for Biomedical Innovation at Harbor-UCLA Medical Center, 1124 West Carson Street, Torrance, CA, 90502, USA.
University of California, Los Angeles · USCalifornia Institute of Technology · USUCLA Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundOptimal functionality of synthetic lung surfactant for treatment of respiratory distress syndrome in preterm infants largely depends on the quality and quantity of the surfactant protein B (SP-B) peptide mimic and the lipid mixture. B-YL peptide is a 41-residue sulfur-free SP-B mimic with its cysteine and methionine residues replaced by tyrosine and leucine, respectively, to enhance its oxidation resistance.

aimTesting the structural and functional stability of the B-YL peptide in synthetic surfactant lipids after long-term storage.

methodsThe structural and functional properties of B-YL peptide in surfactant lipids were studied using three production runs of B-YL peptides in synthetic surfactant lipids. Each run was held at 5 °C ambient temperature for three years and analyzed with structural and computational techniques, i.e., MALDI-TOF mass spectrometry, ATR-Fourier Transform Infrared Spectroscopy (ATR-FTIR), secondary homology modeling of a preliminary B-YL structure, and tertiary Molecular Dynamic simulations of B-YL in surfactant lipids, and with functional methods, i.e., captive bubble surfactometry (CBS) and retesting in vivo surface activity in surfactant-deficient young adult rabbits.

resultsMALDI-TOF mass spectrometry showed no degradation of the B-YL peptide as a function of stored time. ATR-FTIR studies demonstrated that the B-YL peptide still assumed stable alpha-helical conformations in synthetic surfactant lipids. These structural findings correlated with excellent in vitro surface activity during both quasi-static and dynamic cycling on CBS after three years of cold storage and in vivo surface activity of the aged formulations with improvements in oxygenation and dynamic lung compliance approaching those of the positive control surfactant Curosurf®.

conclusionsThe structure of the B-YL peptide and the in vitro and in vivo functions of the B-YL surfactant were each maintained after three years of refrigeration storage.

Indexed as

AnimalsDrug StabilityLipid MetabolismPulmonary Surfactant-Associated Protein BPulmonary SurfactantsRabbitsSurface-Active AgentsPulmonary Surfactant-Associated Protein BPulmonary SurfactantsSurface-Active AgentsB-YL peptideCaptive bubble surfactometryFourier-Transform InfraRed SpectroscopyHomology modelingMass spectroscopyMolecular dynamicsSurfactant-deficient rabbitsSurfactant protein BSynthetic lung surfactant

Identifiers

PMID34686153
PMCPMC8540162
OpenAlexW3207198683

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.