Evidence map›Paper›PMID 28744580›Full record

ArticleAmino acids2017

Stabilization of Angiotensin-(1-7) by key substitution with a cyclic non-natural amino acid.

Anita Wester, Marc Devocelle, E Ann Tallant, Mark C Chappell, Patricia E Gallagher, Francesca Paradisi

Open access · greenAbstract read
In one paragraph

Article in Amino acids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

8 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. 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

6 authors at 3 institutions in 3 countries.

Anita WesterSchool of Chemistry, University College Dublin, Dublin, Ireland.
Marc DevocelleDepartment of Pharmaceutical and Medicinal Chemistry, Centre for Synthesis and Chemical Biology, Royal College of Surgeons in Ireland, Dublin, Ireland.
E Ann TallantSurgery/Hypertension and Vascular Research, Wake Forest School of Medicine, Winston-Salem, NC, USA.
Mark C ChappellSurgery/Hypertension and Vascular Research, Wake Forest School of Medicine, Winston-Salem, NC, USA.
Patricia E GallagherSurgery/Hypertension and Vascular Research, Wake Forest School of Medicine, Winston-Salem, NC, USA.
Francesca ParadisiSchool of Chemistry, University College Dublin, Dublin, Ireland. Francesca.Paradisi@nottingham.ac.uk.ORCID 0000-0003-1704-0642
Wake Forest University · USUniversity College Dublin · IERoyal College of Surgeons in Ireland · IE

Funding

Novel Angiotensin-(1-7) Endopeptidase in Fetal ProgrammingR21HD084227 · NICHD · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI CHAPPELL, MARK C, ROSE, JAMES C. · 2016 to 2017
$426k
American Heart Association AHA-151521 and AHA-355741NICHD NIH HHS R21 HD084227NIH HHS HD084227Science Foundation Ireland 06/RFP/CHO024/EC07
6 · The paper itself

Abstract

Angiotensin-(1-7) [Ang-(1-7)], a heptapeptide hormone of the renin-angiotensin-aldosterone system, is a promising candidate as a treatment for cancer that reflects its anti-proliferative and anti-angiogenic properties. However, the peptide's therapeutic potential is limited by the short half-life and low bioavailability resulting from rapid enzymatic metabolism by peptidases including angiotensin-converting enzyme (ACE) and dipeptidyl peptidase 3 (DPP 3). We report the facile assembly of three novel Ang-(1-7) analogues by solid-phase peptide synthesis which incorporates the cyclic non-natural δ-amino acid ACCA. The analogues containing the ACCA substitution at the site of ACE cleavage exhibit complete resistance to human ACE, while substitution at the DDP 3 cleavage site provided stability against DPP 3 hydrolysis. Furthermore, the analogues retain the anti-proliferative properties of Ang-(1-7) against the 4T1 and HT-1080 cancer cell lines. These results suggest that ACCA-substituted Ang-(1-7) analogues which show resistance against proteolytic degradation by peptidases known to hydrolyze the native heptapeptide may be novel therapeutics in the treatment of cancer.

Indexed as

Amino Acid SubstitutionAngiotensin IPeptide FragmentsProteolysisDipeptidyl-Peptidases and Tripeptidyl-PeptidasesHumansPeptidyl-Dipeptidase AProtein StabilityAngiotensin Iangiotensin I (1-7)Dipeptidyl-Peptidases and Tripeptidyl-PeptidasesDPP3 protein, humanPeptide FragmentsPeptidyl-Dipeptidase AACCAAngiotensin-(1–7)Angiotensin-converting enzymeDipeptidyl peptidase 3Non-natural amino acidPeptidomimetic

Identifiers

PMID28744580
PMCPMC9239115
OpenAlexW2738050484

What OpenQuestion holds

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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.