Evidence map›Paper›PMID 26495044›Full record

ArticleCellular and molecular bioengineering2015

Self-assembled glycopeptide nanofibers as modulators of galectin-1 bioactivity.

Antonietta Restuccia, Ye F Tian, Joel H Collier, Gregory A Hudalla

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular bioengineering, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  8. Physical tuning of galectin-3 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Review
  10. Article
  11. Article
  12. Current Progress in Cross-Linked Peptide Self-Assemblies.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
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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 3 institutions in 1 country.

Antonietta RestucciaJ. Crayton Pruitt Family Department of Biomedical Engineering.
Ye F TianDepartment of Surgery, University of Chicago. ; Department of Biomedical Engineering, Illinois Institute of Technology.
Joel H CollierDepartment of Surgery, University of Chicago.
Gregory A HudallaJ. Crayton Pruitt Family Department of Biomedical Engineering. ; Department of Surgery, University of Chicago.
University of Florida · USIllinois Institute of Technology · USUniversity of Chicago · US

Funding

Theranostic Magnetic Nanostructures for the Molecular Imaging of CancerU54CA151880 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MEADE, THOMAS J · 2010 to 2014
$11.5M
Modular Self-Assembled Coatings for BiomaterialsR01EB009701 · NIBIB · UNIVERSITY OF CHICAGO · PI COLLIER, JOEL H · 2009 to 2021
$4.3M
Molecular assemblies as immunomodulatorsF32AI096769 · NIAID · UNIVERSITY OF CHICAGO · PI HUDALLA, GREGORY · 2011 to 2012
$101k
NCI NIH HHS U54 CA151880NIAID NIH HHS F32 AI096769NIBIB NIH HHS R01 EB009701
6 · The paper itself

Abstract

Galectins are carbohydrate-binding proteins that act as extracellular signaling molecules in various normal and pathological processes. Galectin bioactivity is mediated by specific non-covalent interactions with cell-surface and extracellular matrix (ECM) glycoproteins, which can enhance or inhibit signaling events that influence various cellular behaviors, including adhesion, proliferation, differentiation, and apoptosis. Here, we developed a materials approach to modulate galectin bioactivity by mimicking natural galectin-glycoprotein interactions. Specifically, we created a variant of a peptide that self-assembles into β-sheet nanofibers under aqueous conditions, QQKFQFQFEQQ (Q11), which has an asparagine residue modified with the monosaccharide N-acetylglucosamine (GlcNAc) at its N-terminus (GlcNAc-Q11). GlcNAc-Q11 self-assembled into β-sheet nanofibers under similar conditions as Q11. Nanofibrillar GlcNAc moieties were efficiently converted to the galectin-binding disaccharide N-acetyllactosamine (LacNAc) via the enzyme β-1,4-galactosyltransferase and the sugar donor UDP-galactose, while retaining β-sheet structure and nanofiber morphology. LacNAc-Q11 nanofibers bound galectin-1 and -3 in a LacNAc concentration-dependent manner, although nanofibers bound galectin-1 with higher affinity than galectin-3. In contrast, galectin-1 bound weakly to GlcNAc-Q11 nanofibers, while no galectin-3 binding to these nanofibers was observed. Galectin-1 binding to LacNAc-Q11 nanofibers was specific because it could be inhibited by excess soluble β-lactose, a galectin-binding carbohydrate. LacNAc-Q11 nanofibers inhibited galectin-1-mediated apoptosis of Jurkat T cells in a LacNAc concentration-dependent manner, but were unable to inhibit galectin-3 activity, consistent with galectin-binding affinity of the nanofibers. We envision that glycopeptide nanofibers capable of modulating galectin-1 bioactivity will be broadly useful as biomaterials for various medical applications, including cancer therapeutics, immunotherapy, tissue regeneration, and viral prophylaxis.

Identifiers

PMID26495044
PMCPMC4610397
OpenAlexW610804752

What OpenQuestion holds

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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.