Evidence map›Paper›PMID 23750281›Full record

ArticlePloS one2013

A binding-site barrier affects imaging efficiency of high affinity amyloid-reactive peptide radiotracers in vivo.

Jonathan S Wall, Angela Williams, Tina Richey, Alan Stuckey, Ying Huang, Craig Wooliver, Sallie Macy, Eric Heidel, Neil Gupta, Angela Lee and 3 more

Abstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Conjugate of Doxorubicin to Albumin-Binding Peptide Outperforms Aldoxorubicin.Small (Weinheim an der Bergstrasse, Germany) · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The pattern recognition reagents RAGE VC1 and peptide p5 share common binding sites and exhibit specific reactivity with AA amyloid in mice.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Phagocyte depletion inhibits AA amyloid accumulation in AEF-induced huIL-6 transgenic mice.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2014
    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

13 authors.

Jonathan S WallDepartment of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, Tennessee, USA. jwall@utmck.edu
Angela Williams
Tina Richey
Alan Stuckey
Ying Huang
Craig Wooliver
Sallie Macy
Eric Heidel
Neil Gupta
Angela Lee
Brianna Rader
Emily B Martin
Stephen J Kennel

Funding

Preclinical Diagnostic Imaging of AmyloidR01DK079984 · NIDDK · UNIVERSITY OF TENNESSEE KNOXVILLE · PI WALL, JONATHAN S · 2009 to 2016
$3.4M
NIDDK NIH HHS R01 DK079984NIDDK NIH HHS R01DK079984
6 · The paper itself

Abstract

Amyloid is a complex pathology associated with a growing number of diseases including Alzheimer's disease, type 2 diabetes, rheumatoid arthritis, and myeloma. The distribution and extent of amyloid deposition in body organs establishes the prognosis and can define treatment options; therefore, determining the amyloid load by using non-invasive molecular imaging is clinically important. We have identified a heparin-binding peptide designated p5 that, when radioiodinated, was capable of selectively imaging systemic visceral AA amyloidosis in a murine model of the disease. The p5 peptide was posited to bind effectively to amyloid deposits, relative to similarly charged polybasic heparin-reactive peptides, because it adopted a polar α helix secondary structure. We have now synthesized a variant, p5R, in which the 8 lysine amino acids of p5 have been replaced with arginine residues predisposing the peptide toward the α helical conformation in an effort to enhance the reactivity of the peptide with the amyloid substrate. The p5R peptide had higher affinity for amyloid and visualized AA amyloid in mice by using SPECT/CT imaging; however, the microdistribution, as evidenced in micro-autoradiographs, was dramatically altered relative to the p5 peptide due to its increased affinity and a resultant "binding site barrier" effect. These data suggest that radioiodinated peptide p5R may be optimal for the in vivo detection of discreet, perivascular amyloid, as found in the brain and pancreatic vasculature, by using molecular imaging techniques; however, peptide p5, due to its increased penetration, may yield more quantitative imaging of expansive tissue amyloid deposits.

Indexed as

Amino Acid SequenceAmyloidAnimalsBinding SitesHeparinImmobilized ProteinsMiceModels, MolecularMolecular ImagingMolecular Sequence DataPeptidesProtein BindingProtein Structure, SecondaryRadioactive TracersSpleenTomography, Emission-Computed, Single-PhotonAmyloidHeparinImmobilized ProteinsPeptidesRadioactive Tracers

Identifiers

PMID23750281
PMCPMC3672142

What OpenQuestion holds

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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.