Evidence map›Paper›PMID 33289741›Full record

ArticleBiomaterials science2021

Receptor mimicking TGF-β1 binding peptide for targeting TGF-β1 signaling.

David G Belair, Jae Sung Lee, Anna V Kellner, Johnny Huard, William L Murphy

Open access · greenAbstract read
In one paragraph

Article in Biomaterials science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. Amelioration of Liver Fibrosis via In Situ Hepatic Stellate Cell Conversion Through Co-Inhibition of TGF-β and GSK-3 Signalling.Liver international : official journal of the International Association for the Study of the Liver · 2025
    Article
  4. 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

5 authors at 2 institutions in 2 countries.

David G BelairDepartment of Biomedical Engineering, University of Wisconsin-Madison, Madison, WI, USA. wlmurphy@wisc.edu.ORCID http://orcid.org/0000-0003-2145-3829
Jae Sung LeeDepartment of Orthopedics and Rehabilitation, University of Wisconsin-Madison, Madison, WI, USA.ORCID http://orcid.org/0000-0001-6451-5386
Anna V KellnerSchool of Pharmacy, University of Wisconsin-Madison, Madison, WI, USA.ORCID http://orcid.org/0000-0003-0104-5334
Johnny HuardCenter for Regenerative Sports Medicine, Steadman Philippon Research Institute, Vail, CO, USA.
William L MurphyDepartment of Biomedical Engineering, University of Wisconsin-Madison, Madison, WI, USA. wlmurphy@wisc.edu and Department of Orthopedics and Rehabilitation, University of Wisconsin-Madison, Madison, WI, USA and Materials Science Program, University of Wisconsin-Madison, Madison, WI, USA.ORCID http://orcid.org/0000-0001-5577-7739
University of Wisconsin–Madison · USSteadman Philippon Research Institute · US

Funding

Training Program in Translational Cardiovascular Science (TPTCS)T32HL007936 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Lee Lochbaum Eckhardt, Gail A Robertson · 2001 to 2026
$11.6M
Harnessing human brain and liver microphysiological systems for testing therapeutics for metastatic melanomaU01TR002383 · NCATS · VANDERBILT UNIVERSITY · PI MURPHY, WILLIAM L., TAYLOR, D. LANSING · 2018 to 2022
$7.6M
Biomaterials for local regulation of growth factor signalingR01HL093282 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MURPHY, WILLIAM L. · 2009 to 2018
$3.3M
A Neurovascular Microphysiological SystemR01NS109427 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI MURPHY, WILLIAM L. · 2019 to 2023
$1.7M
Probing biochemical/biophysical influences on endothelial-mesenchymal transitionR21EB016381 · NIBIB · UNIVERSITY OF WISCONSIN-MADISON · PI MURPHY, WILLIAM L., SCHWARTZ, MICHAEL PAUL · 2013 to 2014
$399k
ACQUISITION OF MASS SPECTROMETER FOR CORE FACILITYS10RR013790 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI RAINES, RONALD T · 1999 to 1999
–
NCATS NIH HHS U01 TR002383NCRR NIH HHS S10 RR013790NHLBI NIH HHS R01 HL093282NHLBI NIH HHS T32 HL007936NIBIB NIH HHS R21 EB016381NINDS NIH HHS R01 NS109427
6 · The paper itself

Abstract

Prolonged and elevated transforming growth factor-β1 (TGF-β1) signaling can lead to undesired scar formation during tissue repair and fibrosis that is often a result of chronic inflammation in the lung, kidney, liver, heart, skin, and joints. We report new TGF-β1 binding peptides that interfere with TGF-β1 binding to its cognate receptors and thus attenuate its biological activity. We identified TGF-β1 binding peptides from the TGF-β1 binding domains of TGF-β receptors and engineered their sequences to facilitate chemical conjugation to biomaterials using molecular docking simulations. The in vitro binding studies and cell-based assays showed that RIPΔ, which was derived from TGF-β type I receptor, bound TGF-β1 in a sequence-specific manner and reduced the biological activity of TGF-β1 when the peptide was presented either in soluble form or conjugated to a commonly used synthetic biomaterial. This approach may have implications for clinical applications such as treatment of various fibrotic diseases and soft tissue repair and offer a design strategy for peptide antibodies based on the biomimicry of ligand-receptor interactions.

Indexed as

Receptors, Transforming Growth Factor betaTransforming Growth Factor beta1Molecular Docking SimulationPeptidesSignal TransductionPeptidesReceptors, Transforming Growth Factor betaTransforming Growth Factor beta1

Identifiers

PMID33289741
PMCPMC9254699
OpenAlexW3112008255

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.