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Cited by 8Blood properties and coagulationSupramolecular Self-Assembly in MaterialsSilk-based biomaterials and applications

Thrombin-Free Fibrillogenesis and Gelation of Fibrinogen Triggered by Magnesium Sulfate

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Hense, Dominik, Strube, Oliver I.·2023·Gels
DOI 10.3390/gels9110892PMC PMC10671114
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Abstract

Self-assembly of the blood protein fibrinogen is a highly relevant topic in materials science and medical research. This originates from fibrinogen’s beneficial material properties such as cell interaction and biocompatibility. Within recent decades, several enzyme-free strategies to create fibers and hydrogels out of fibrinogen have been presented, broadening the spectrum of fibrinogen-based material enormously. Herein, we describe a further method to obtain such a material by adding specifically MgSO4 to fibrinogen. The key of this material is the combination of Mg2+ and a kosmotropic anion, for example sulfate or (hydrogen)phosphate. This effect is most likely related to occupancy of fibrinogen’s well-known binding sites for Mg2+, resulting in a significant increase in fiber yield and gel stability. Here, we shine light on the question of how electrostatic interactions via Mg2+ enhance fibrillogenesis and the gelation of fibrinogen and discuss first insights into the material’s properties.

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  • A significant impediment to the broad adoption of fibrin-based barriers is the considerable challenges and expenses inherent in their large-scale manufacturing, considering the fibrin molecule's origin in blood plasma.

    “Consequently, a significant impediment to the broad adoption of fibrin-based barriers stems from the considerable challenges and expenses inherent in their large-scale manufacturing, considering the fibrin molecule’s origin in blood plasma [78,79].”

    From Biomaterials in Postoperative Adhesion Barriers and Uterine Tissue Engineering (2025) · cites this paper as [78]

    The Introduction identifies cost as a downside of fibrin and discusses inexpensive thrombin-free alternatives. It does not attribute that cost to fibrinogen’s origin in blood plasma or discuss large-scale manufacturing; instead, it calls isolation of fibrinogen and thrombin comparatively uncomplicated. (LLM, conf=0.85)

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Cited by

Sorted by citations

Authors
Hense, D., & Strube, O. I.
Affiliations
Universität Innsbruck (AT)
Corresponding author
Strube, Oliver I.
ORCID
Strube, Oliver I.
Venue
Gels
Publisher
MDPI AG
Published
2023-11-11
Volume
9
Issue
11
Pages
892
ISSN
2310-2861 (ISSN-L)
DOI
10.3390/gels9110892
PMC
PMC10671114
OpenAlex
W4388637935
Cited by
8
References
0
Citations by year
2026: 3 · 2025: 2 · 2024: 3
FWCI
1.42
Type
journal article
Language
en
Open access
Licence
Locations
  • Gels (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics
  • Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Blood properties and coagulation
  • Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
Keywords
fibrinogen, fibril formation, gelation, magnesium sulfate, magnesium binding sites, kosmotropic anions, sulfate, phosphate, electrostatic interactions, fiber yield, gel stability

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