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

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.

SUBMITTER: Hense D

PROVIDER: S-EPMC10671114 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature

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

Hense Dominik D Strube Oliver I OI

Gels (Basel, Switzerland) 20231111 11

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 specifical ...[more]

PMID: 37998982

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