Level D· Scientific groundwork from lab and animal studiesLaboratory StudyEurope PMCOpen access

Recombinant Fibrinogen-Gamma-Chain as a Crosslinker of Thiol-ene Hydrogels

Schlauch D., Güler CS., Harzi M., Kara S., Lavrentieva A., Pepelanova I.

Laboratory Study, published in Biopolymers (2026) — summary generated from the PubMed abstract.

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Level D· Scientific groundwork from lab and animal studiesEvidence level of this study

Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.

  • Level A · Stronger Clinical Evidence
  • Level B · Emerging clinical evidence with positive signals
  • Level C · Early human research exploring benefits
  • Level D · Scientific groundwork from lab and animal studies
  • Emerging · Emerging topic under active research
Read the A–D evidence level guide

This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.

Study type
Laboratory Study
Journal
Biopolymers (2026)
Reported sample size
—
Source database
Europe PMC
PMID
41933468
PMCID
PMC13049249
DOI
10.1002/bip.70097

Abstract (original English)

Hydrogels based on thiol-ene step-growth chemistry have gained increased attention due to their superior properties over the currently standard materials based on chain growth polymerization. In the thiol-ene reaction, a crosslinker with at least two thiol groups is necessary for network formation. Many currently used crosslinkers exhibit cytotoxic potential, are non-biodegradable, or involve toxic chemicals and relatively complicated procedures in their synthesis, thus hindering their broader application. As an alternative, the use of a protein (fibrinogen gamma chain, FGG) recombinantly expressed in Escherichia coli was investigated. The FGG is part of the multimeric fibrinogen involved in hemostasis. This protein complex is stabilized by disulfide crosslinking. This presence of cysteines in the sequence makes FGG a promising candidate as a thiol donor in thiol-ene reactions. It was shown for the first time, that a cysteine-containing protein expressed in E. coli was capable of forming hydrogels with norbornene functionalized gelatin. An increase in FGG concentration led to higher gel stiffness and a decrease in the swelling ratio. Furthermore, the material exhibited cell adhesive properties and biocompatibility. Overall, a proof-of-principle could be achieved, opening up the use of recombinant proteins without further modifications as crosslinkers in thiol-ene based hydrogel

What this study does not prove

  • • This study does not prove SVF is an approved treatment or a replacement for standard care.
  • • This is preclinical work; animal or laboratory results cannot be applied to humans.

Evidence level

Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.

How we grade evidence
Escherichia coliNorbornanesSulfhydryl CompoundsFibrinogenRecombinant ProteinsGelatinHydrogelsCross-Linking ReagentsCell Adhesion

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