Evidence map›Paper›PMID 38968389›Full record

ArticleACS biomaterials science & engineering2024

Quantifying and Controlling the Proteolytic Degradation of Cell Adhesion Peptides.

Samuel J Rozans, Abolfazl Salehi Moghaddam, Yingjie Wu, Kayleigh Atanasoff, Liliana Nino, Katelyn Dunne, E Thomas Pashuck

Abstract read
In one paragraph

Article in ACS biomaterials science & engineering, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. The Rise of Mechanobiology for Advanced Cell Engineering and Manufacturing.Advanced materials (Deerfield Beach, Fla.) · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Samuel J RozansDepartment of Bioengineering, Lehigh University, 7 Asa Drive, Suite 205, Bethlehem, PA 18015, United States.ORCID 0009-0003-2688-510X
Abolfazl Salehi MoghaddamDepartment of Bioengineering, Lehigh University, 7 Asa Drive, Suite 205, Bethlehem, PA 18015, United States.
Yingjie WuDepartment of Bioengineering, Lehigh University, 7 Asa Drive, Suite 205, Bethlehem, PA 18015, United States.
Kayleigh AtanasoffDepartment of Bioengineering, Lehigh University, 7 Asa Drive, Suite 205, Bethlehem, PA 18015, United States.
Liliana NinoDepartment of Bioengineering, Lehigh University, 7 Asa Drive, Suite 205, Bethlehem, PA 18015, United States.
Katelyn DunneDepartment of Bioengineering, Lehigh University, 7 Asa Drive, Suite 205, Bethlehem, PA 18015, United States.
E Thomas PashuckDepartment of Bioengineering, Lehigh University, 7 Asa Drive, Suite 205, Bethlehem, PA 18015, United States.ORCID 0000-0003-2881-4965

Funding

Designing technologies to visualize protease activity in cancer modelsR21GM143593 · NIGMS · LEHIGH UNIVERSITY · PI PASHUCK, EUGENE THOMAS · 2021 to 2022
$408k
Designing Hydrogels that Recapitulate Physiological Cell-Matrix AdhesionsR03EB036263 · NIBIB · LEHIGH UNIVERSITY · PI PASHUCK, EUGENE THOMAS · 2024 to 2025
$144k
NIBIB NIH HHS R03 EB036263NIGMS NIH HHS R21 GM143593
6 · The paper itself

Abstract

Peptides are widely used within biomaterials to improve cell adhesion, incorporate bioactive ligands, and enable cell-mediated degradation of the matrix. While many of the peptides incorporated into biomaterials are intended to be present throughout the life of the material, their stability is not typically quantified during culture. In this work, we designed a series of peptide libraries containing four different N-terminal peptide functionalizations and three C-terminal functionalizations to better understand how simple modifications can be used to reduce the nonspecific degradation of peptides. We tested these libraries with three cell types commonly used in biomaterials research, including mesenchymal stem/stromal cells (hMSCs), endothelial cells, and macrophages, and quantified how these cell types nonspecifically degraded peptides as a function of terminal amino acid and chemistry. We found that peptides in solution which contained N-terminal amines were almost entirely degraded by 48 h, irrespective of the terminal amino acid, and that degradation occurred even at high peptide concentrations. Peptides with C-terminal carboxylic acids also had significant degradation when cultured with the cells. We found that simple modifications to the termini could significantly reduce or completely abolish nonspecific degradation when soluble peptides were added to cells cultured on tissue culture plastic or within hydrogel matrices, and that functionalizations which mimicked peptide conjugations to hydrogel matrices significantly slowed nonspecific degradation. We also found that there were minimal differences in peptide degradation across cell donors and that sequences mimicking different peptides commonly used to functionalize biomaterials all had significant nonspecific degradation. Finally, we saw that there was a positive trend between RGD stability and hMSC spreading within hydrogels, indicating that improving the stability of peptides within biomaterial matrices may improve the performance of engineered matrices.

Indexed as

Cell AdhesionMesenchymal Stem CellsPeptidesProteolysisAnimalsBiocompatible MaterialsHumansHydrogelsMacrophagesMicePeptide LibraryBiocompatible MaterialsHydrogelsPeptide LibraryPeptidesbioavailabilitybiomaterialsexopeptidaseLCMSproteaseRGD

Identifiers

PMID38968389
PMCPMC11322908

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.