Evidence map›Paper›PMID 41279057›Full record

ArticlebioRxiv : the preprint server for biology2025

Design and Synthesis of Peptide-Polyester Conjugates for Cell-Mediated Scaffold Degradation.

Korina Vida G Sinad, Natasha K Hunt, Srujan Singh, Kelly B Seims, Yingjie Wu, E Thomas Pashuck, Warren L Grayson, Lesley W Chow

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Korina Vida G SinadDepartment of Chemistry, Lehigh University, Bethlehem, PA, USA.ORCID 0009-0004-4488-5506
Natasha K HuntDepartment of Bioengineering, Lehigh University, Bethlehem, PA, USA.ORCID 0009-0003-8176-3631
Srujan SinghDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0002-7498-4298
Kelly B SeimsDepartment of Materials Science & Engineering, Lehigh University, Bethlehem, PA, USA.ORCID 0000-0002-6345-753X
Yingjie WuDepartment of Bioengineering, Lehigh University, Bethlehem, PA, USA.ORCID 0009-0005-8410-6041
E Thomas PashuckDepartment of Bioengineering, Lehigh University, Bethlehem, PA, USA.ORCID 0000-0003-2881-4965
Warren L GraysonDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0001-6099-6469
Lesley W ChowDepartment of Bioengineering, Lehigh University, Bethlehem, PA, USA.ORCID 0000-0001-5252-2239

Funding

Oxygen-eluting scaffolds for cranial bone regenerationR01DE027957 · NIDCR · JOHNS HOPKINS UNIVERSITY · PI GRAYSON, WARREN L, PATHAK, ARVIND P · 2019 to 2023
$2.4M
NIDCR NIH HHS R01 DE027957
6 · The paper itself

Abstract

Biodegradable thermoplastic polyesters are promising biomaterials for tissue engineering due to their processability and mechanical properties. Polycaprolactone (PCL) is particularly attractive for load-bearing applications but does not degrade at the same rate as new tissue formation, which may compromise functional regeneration. This study presents a strategy for cell-mediated scaffold remodeling by incorporating a protease-cleavable peptide directly into the PCL backbone. Linear peptide-PCL conjugates were synthesized with poly(ethylene glycol) (PEG) spacers flanking the peptide to enhance protease access. A functional proteomics approach was used to identify a fast-degrading peptide sequence (Fast) selectively cleaved by multiple cell types. Conjugates containing Fast or its scrambled control (ScrFast) were combined with an RGDS-PCL conjugate and fabricated into scaffolds. Including Fast and ScrFast peptides did not impair cell adhesion to the scaffolds. Cy3 labeling enabled real-time quantification of scaffold degradation in the presence of collagenase or human mesenchymal stromal cells (hMSCs). Fast-PCL scaffolds degraded significantly faster than ScrFast-PCL in both conditions, demonstrating sequence-dependent and cell-directed resorption. Integrating protease-sensitive peptides into the polymer backbone is therefore an effective approach to fabricate solid scaffolds that degrade in response to cells. This platform can be adapted to couple cellular processes to scaffold remodeling to enhance tissue regeneration.

Indexed as

biodegradable polymersbiomaterialscell-mediated degradationpeptidesproteasestissue engineering

Identifiers

PMID41279057
PMCPMC12632545

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.