Evidence map›Paper›PMID 30415064›Full record

ArticleActa biomaterialia2019

Dynamic control of hydrogel crosslinking via sortase-mediated reversible transpeptidation.

Matthew R Arkenberg, Dustin M Moore, Chien-Chi Lin

Abstract read
In one paragraph

Article in Acta biomaterialia, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Enzymatic Methods for Assembling and Modifying Hydrogel Biomaterials.Regenerative engineering and translational medicine · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Engineered Protein Hydrogels as Biomimetic Cellular Scaffolds.Advanced materials (Deerfield Beach, Fla.) · 2024
    Review
  14. Review
  15. Chemical and Photochemical-Driven Dissipative FeJournal of the American Chemical Society · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors at 1 institution in 1 country.

Matthew R ArkenbergDepartment of Biomedical Engineering, Purdue School of Engineering & Technology, Indiana University-Purdue University Indianapolis, Indianapolis, IN 46202, USA.
Dustin M MooreDepartment of Biomedical Engineering, Purdue School of Engineering & Technology, Indiana University-Purdue University Indianapolis, Indianapolis, IN 46202, USA.
Chien-Chi LinDepartment of Biomedical Engineering, Purdue School of Engineering & Technology, Indiana University-Purdue University Indianapolis, Indianapolis, IN 46202, USA. Electronic address: lincc@iupui.edu.
University of Indianapolis · US

Funding

Translation CoreP30DK097512 · NIDDK · INDIANA UNIVERSITY INDIANAPOLIS · PI Carmella Evans-Molina · 2015 to 2026
$17.4M
Interdisciplinary Bioengineering Training in Diabetes ResearchT32DK101001 · NIDDK · PURDUE UNIVERSITY · PI EVANS-MOLINA, CARMELLA, VOYTIK-HARBIN, SHERRY L · 2013 to 2022
$1.6M
NIDDK NIH HHS P30 DK097512NIDDK NIH HHS T32 DK101001
6 · The paper itself

Abstract

Cell-laden hydrogels whose crosslinking density can be dynamically and reversibly tuned are highly sought-after for studying pathophysiological cellular fate processes, including embryogenesis, fibrosis, and tumorigenesis. Special efforts have focused on controlling network crosslinking in poly(ethylene glycol) (PEG) based hydrogels to evaluate the impact of matrix mechanics on cell proliferation, morphogenesis, and differentiation. In this study, we sought to design dynamic PEG-peptide hydrogels that permit cyclic/reversible stiffening and softening. This was achieved by utilizing reversible enzymatic reactions that afford specificity, biorthogonality, and predictable reaction kinetics. To that end, we prepared PEG-peptide conjugates to enable sortase A (SrtA) induced tunable hydrogel crosslinking independent of macromer contents. Uniquely, these hydrogels can be completely degraded by the same enzymatic reactions and the degradation rate can be tuned from hours to days. We further synthesized SrtA-sensitive peptide linker (i.e., KCLPRTGCK) for crosslinking with 8-arm PEG-norbornene (PEG8NB) via thiol-norbornene photocrosslinking. These hydrogels afford diverse softening paradigms through control of network structures during crosslinking or by adjusting enzymatic parameters during on-demand softening. Importantly, user-controlled hydrogel softening promoted spreading of human mesenchymal stem cells (hMSCs) in 3D. Finally, we designed a bis-cysteine-bearing linear peptide flanked with SrtA substrates at the peptide's N- and C-termini (i.e., NH

Indexed as

AminoacyltransferasesBacterial ProteinsCross-Linking ReagentsCysteine EndopeptidasesHumansHydrogelsMesenchymal Stem CellsPeptidesAminoacyltransferasesBacterial ProteinsCross-Linking ReagentsCysteine EndopeptidasesHydrogelsPeptidessortase ACancerDynamic hydrogelsExtracellular matrixSortase ATissue stiffening

Identifiers

PMID30415064
PMCPMC6697659
OpenAlexW2900058404

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.