Evidence map›Paper›PMID 37350860›Full record

ArticleRSC advances2023

Stability and structure-activity relationship of the SPA4 peptide under ambient and stressed conditions of lung injury.

Asif Alam Chowdhury, Karla Rodgers, Nachiket M Godbole, Shanjana Awasthi

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 40% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Article
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 1 institution in 1 country.

Asif Alam ChowdhuryDepartment of Pharmaceutical Sciences, University of Oklahoma Health Sciences Center 1110 N. Stonewall Avenue Oklahoma City OK-73117 USA Shanjana-Awasthi@ouhsc.edu +1-405-271-7505 +1-405-271-6593 extn 47332.ORCID https://orcid.org/0000-0001-5470-7405
Karla RodgersDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center 940 Stanton L. Young Blvd Oklahoma City OK-73104 USA.ORCID https://orcid.org/0000-0002-7338-0281
Nachiket M GodboleDepartment of Pharmaceutical Sciences, University of Oklahoma Health Sciences Center 1110 N. Stonewall Avenue Oklahoma City OK-73117 USA Shanjana-Awasthi@ouhsc.edu +1-405-271-7505 +1-405-271-6593 extn 47332.ORCID https://orcid.org/0009-0001-2388-8554
Shanjana AwasthiDepartment of Pharmaceutical Sciences, University of Oklahoma Health Sciences Center 1110 N. Stonewall Avenue Oklahoma City OK-73117 USA Shanjana-Awasthi@ouhsc.edu +1-405-271-7505 +1-405-271-6593 extn 47332.ORCID https://orcid.org/0000-0003-1249-0708
University of Oklahoma Health Sciences Center · US

Funding

Surfactant protein-A regions as TLR4-immunomodulatorsR01HL136325 · NHLBI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI AWASTHI, SHANJANA · 2017 to 2021
$1.8M
NHLBI NIH HHS R01 HL136325
6 · The paper itself

Abstract

Lung inflammation and injuries are major health problems. The SPA4 peptide (amino acid sequence GDFRYSDGTPVNYTNWYRGE) binds to Toll-like receptor-4 and exerts anti-inflammatory activity. In this study, we have determined the stability of the structure and structure-activity relationship of the SPA4 peptide under ambient and stressed conditions of lung injury. The SPA4 peptide was maintained at different pH and temperatures, in solutions of different ionic strengths, and simulated lung fluids. The primary and secondary structure of the SPA4 peptide was determined by ultraviolet-visible (UV-VIS) and circular dichroism (CD) spectroscopy. The activity of the SPA4 peptide was determined by measurement of secreted levels of chemokine C-X-C motif ligand 1/keratinocyte-derived chemokine (CXCL1/KC) and lactate by primary mouse lung epithelial cells against lipopolysaccharide (LPS) stimuli. Our results demonstrate the stability of the structure of the SPA4 peptide at room temperature and 4 °C over 10 days. The original UV-VIS spectra of the SPA4 peptide followed a typical pattern when incubated in solutions of pH 5.7, 7.0, and 8.0 at different temperatures, simulated lung fluids, and most of the chemical components. Slight shifts in the absorbance peaks, derivative values, and vibrational fine structures were noted in the fourth-derivative spectra of the SPA4 peptide under some conditions. An increased level of lactate is the hallmark of lung injury. The SPA4 peptide on its own and in the presence of lactate exerts anti-inflammatory activity. The primary and secondary structure and the activity of the SPA4 peptide remain intact when pre-incubated in 2 mM sodium lactate solution. The results provide important insights about the stability and structure-activity relationship of the SPA4 peptide.

Identifiers

PMID37350860
PMCPMC10282593
OpenAlexW4381663910

What OpenQuestion holds

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LicenceCC BY-NC
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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.