Evidence map›Paper›PMID 31611567›Full record

ArticleScientific reports2019

Molecular insights into the interaction of hemorphin and its targets.

Amanat Ali, Bincy Baby, Soja Saghar Soman, Ranjit Vijayan

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Computational Modeling of the Interactions between DPP IV and Hemorphins.International journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Peptidomics.Nature reviews. Methods primers · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Hemorphins-From Discovery to Functions and Pharmacology.Molecules (Basel, Switzerland) · 2021
    Review
  14. Hemorphins Targeting G Protein-Coupled Receptors.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Review
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 2 institutions in 1 country.

Amanat AliDepartment of Biology, College of Science, United Arab Emirates University, PO Box 15551, Al Ain, Abu Dhabi, United Arab Emirates.
Bincy BabyDepartment of Biology, College of Science, United Arab Emirates University, PO Box 15551, Al Ain, Abu Dhabi, United Arab Emirates.
Soja Saghar SomanNew York University Abu Dhabi, PO Box 129188, Abu Dhabi, United Arab Emirates.
Ranjit VijayanDepartment of Biology, College of Science, United Arab Emirates University, PO Box 15551, Al Ain, Abu Dhabi, United Arab Emirates. ranjit.v@uaeu.ac.ae.
United Arab Emirates University · AENew York University Abu Dhabi · AE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hemorphins are atypical endogenous opioid peptides produced by the cleavage of hemoglobin beta chain. Several studies have reported the therapeutic potential of hemorphin in memory enhancement, blood regulation, and analgesia. However, the mode of interaction of hemorphin with its target remains largely elusive. The decapeptide LVV-hemorphin-7 is the most stable form of hemorphin. It binds with high affinity to mu-opioid receptors (MOR), angiotensin-converting enzyme (ACE) and insulin-regulated aminopeptidase (IRAP). In this study, computational methods were used extensively to elucidate the most likely binding pose of mammalian LVV-hemorphin-7 with the aforementioned proteins and to calculate the binding affinity. Additionally, alignment of mammalian hemorphin sequences showed that the hemorphin sequence of the camel harbors a variation - a Q > R substitution at position 8. This study also investigated the binding affinity and the interaction mechanism of camel LVV-hemorphin-7 with these proteins. To gain a better understanding of the dynamics of the molecular interactions between the selected targets and hemorphin peptides, 100 ns molecular dynamics simulations of the best-ranked poses were performed. Simulations highlighted major interactions between the peptides and key residues in the binding site of the proteins. Interestingly, camel hemorphin had a higher binding affinity and showed more interactions with all three proteins when compared to the canonical mammalian LVV-hemorphin-7. Thus, camel LVV-hemorphin-7 could be explored as a potent therapeutic agent for memory loss, hypertension, and analgesia.

Indexed as

Amino Acid SequenceAnimalsHemoglobinsHumansModels, MolecularPeptide FragmentsPeptidyl-Dipeptidase AProtein BindingProtein Interaction Domains and MotifsProtein Interaction MapsReceptors, Opioid, muSequence AlignmentHemoglobinsLVV-hemorphin-7Peptide FragmentsPeptidyl-Dipeptidase AReceptors, Opioid, mu

Identifiers

PMID31611567
PMCPMC6791854
OpenAlexW2980135851

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.