Evidence map›Paper›PMID 29691664›Full record

ArticlePharmaceutical research2018

Characterization of the PEGylated Functional Upstream Domain Peptide (PEG-FUD): a Potent Fibronectin Assembly Inhibitor with Potential as an Anti-Fibrotic Therapeutic.

Pawel Zbyszynski, Bianca R Tomasini-Johansson, Donna M Peters, Glen S Kwon

Open access · greenAbstract read
In one paragraph

Article in Pharmaceutical research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
  5. [Science advances · 2024
    Article
  6. Review
  7. Fibronectin-targeted FUD and PEGylated FUD peptides for fibrotic diseases.Journal of controlled release : official journal of the Controlled Release Society · 2023
    Article
  8. Article
  9. Multimodal imaging demonstrates enhanced tumor exposure of PEGylated FUD peptide in breast cancer.Journal of controlled release : official journal of the Controlled Release Society · 2022
    Article
  10. Article
  11. Article
  12. 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 1 institution in 1 country.

Pawel ZbyszynskiDivision of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Bianca R Tomasini-JohanssonDivision of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Donna M PetersDepartment of Pathology & Laboratory Medicine, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Glen S KwonDivision of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, Wisconsin, USA. gskwon@pharmacy.wisc.edu.
University of Wisconsin–Madison · US

Funding

UW Vision Research Core - Administrative CoreP30EY016665 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERT W NICKELLS · 2005 to 2026
$12.6M
Control of Trabecular Meshwork CytoskeletonR01EY017006 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI PETERS, DONNA M · 2006 to 2024
$6.1M
Co-Delivery of Antifungal Agents: Toxicity and Efficacy in Invasive CandidiasisR01AI101157 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KWON, GLEN S. · 2013 to 2017
$1.9M
Control of ECM HomeostasisR01EY026009 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI PETERS, DONNA M · 2016 to 2019
$1.4M
Integrin Signaling in the Trabecular MeshworkR01EY020490 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI PETERS, DONNA M · 2010 to 2012
$1.1M
NEI NIH HHS EY0020490NEI NIH HHS EY017006NEI NIH HHS P30 EY016665NEI NIH HHS R01 EY017006NEI NIH HHS R01 EY020490NEI NIH HHS R01 EY026009NIAID NIH HHS R01 AI101157NIH HHS R01AI101157
6 · The paper itself

Abstract

purposeTo develop PEGylated variants of pUR4/FUD (FUD), a fibronectin assembly inhibitor, using 10 kDa, 20 kDa, and 40 kDa PEGs to evaluate their binding affinity and inhibitory potency.

methodsThe FUD peptide was recombinantly expressed, purified, and PEGylated at the N-terminus using 10 kDa, 20 kDa, and 40 kDa methoxy-PEG aldehyde. The PEGylates were purified and fractionated using ion-exchange chromatography. The molecular weight and degree of PEGylation of each conjugate was verified using MALDI-TOF. The binding affinity of each PEG-FUD conjugate was studied using isothermal titration colorimetry (ITC) and their inhibitory potency was characterized by a cell-based matrix assembly in vitro assay.

resultsThe 10 kDa, 20 kDa, and 40 kDa PEG-FUD conjugates were synthesized and isolated in good purity as determined by HPLC analysis. Their molecular weight was consistent with attachment of a single PEG molecule to one FUD peptide. The binding affinity (K

conclusionsRetention of FUD fibronectin binding activity following PEGylation with three different PEG sizes suggest that PEG-FUD holds promise as an effective anti-fibrotic with therapeutic potential and a candidate for further pharmacokinetic and biodistribution studies.

Indexed as

Antifibrinolytic AgentsCell SurvivalDose-Response Relationship, DrugFibroblastsFibronectinsHumansMalePeptide FragmentsPolyethylene GlycolsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAntifibrinolytic AgentsFibronectinsPeptide FragmentsPolyethylene GlycolsAnti-fibrosis therapyfibronectinPEGpeptide deliverypUR4/FUD

Identifiers

PMID29691664
PMCPMC6186450
OpenAlexW2801438308

What OpenQuestion holds

Textmetadata
LicenceTDM
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.