Investigation of the affinity and interaction of fibrinogen with trehalose as a protein stabilizer.

[Display omitted] • Fibrinogen, a vital protein involved in wound healing and blood clotting, requires stability for proper functioning. • Trehalose, an effective protein stabilizer, is capable of preserving fibrinogen's structure and functionality. • Through hydrogen bonding and van der Waals forces, trehalose binds to fibrinogen, causing compaction and stability. • Specifically, trehalose primarily attaches to the C-terminal and globular regions of fibrinogen's Bβ chain. • Fibrinogen-trehalose complex exhibited reduced toxicity compared to trehalose alone, highlighting its potential use as a safe and effective protein stabilizer. Trehalose, a remarkable substance, holds great importance in biomedicine for its anti-inflammatory properties and its capacity to hinder scar formation at wounds. This study aims to explore how trehalose interacts with fibrinogen, a crucial protein in wound healing, paying particular attention to their structural characteristics. An array of analytical methods, such as steady-state fluorescence, UV–Vis analysis, circular dichroism (CD), Zeta potential measurements, Dynamic light scattering (DLS), and Fourier-transform infrared spectroscopy (FT-IR), are employed to examine the influence of trehalose on fibrinogen. The findings demonstrate that trehalose induces structural alterations on the surface of fibrinogen, resulting in its compaction. Moreover, computational modeling approaches like docking and molecular dynamics simulations are utilized to enhance the understanding of the interactions between trehalose and fibrinogen. The findings indicate the establishment of a stable complex between the two entities, accompanied by slight modifications in the protein's structure due to their interaction. The main forces facilitating the bonding of trehalose (the ligand) and the protein are hydrogen bonds and van der Waals forces, resulting in an entropy-driven spontaneous bonding process. FT-IR data reveals the emergence of fresh bonds between fibrinogen and trehalose post their interaction, whereas Zeta potential investigations suggest that the engagement with trehalose enhances the stability of the protein structure. Tests assessing cytotoxicity on a typical fibroblast cell line demonstrated that the fibrinogen-trehalose compound displays lower toxicity levels compared to trehalose alone. This suggests a milder impact on cells from the compound. Moreover, molecular docking analysis supports these experimental results, indicating that trehalose molecules primarily bind to the C-terminal end of the coiled-coil segment and the globular area of the Bβ chain within the Dβ fragment. These outcomes highlight the promise of trehalose as a valuable material for wound dressing purposes. [ABSTRACT FROM AUTHOR]