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

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 MgSO to fibrinogen. The key of this material is the combination of Mg 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 Mg, resulting in a significant increase in fiber yield and gel stability. Here, we shine light on the question of how electrostatic interactions via Mg enhance fibrillogenesis and the gelation of fibrinogen and discuss first insights into the material's properties.