Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks

Area of Science:

• Biochemistry
• Biophysics
• Materials Science

Background:

• Fibrin, a key plasma protein, self-assembles into complex networks essential for blood clotting and wound healing.
• Fibrin assembly progresses from monomers to protofibrils and finally to thick fibers, influenced by physicochemical conditions.
• Buffering agents, crucial for pH control, are typically assumed to be inert in biomolecular processes.

Purpose of the Study:

• To investigate the influence of buffering agents on fibrin self-assembly.
• To determine how buffers affect the different stages of fibrin network formation.
• To explore the implications of buffer-mediated effects on fibrin network properties and in vivo assembly.

Main Methods:

• Confocal microscopy to visualize fibrin network structure.
• Quantitative light scattering to analyze fibrin assembly dynamics.
• Experiments conducted with purified fibrin and platelet-poor plasma.

Main Results:

• Common buffering agents do not affect fibrin monomer to protofibril assembly.
• Buffers significantly impede the lateral association of protofibrils into thicker fibers.
• Buffer-induced changes reduce fibrin network permeability with minimal impact on elastic modulus.

Conclusions:

• Buffering agents are not inert and actively modulate fibrin self-assembly, specifically protofibril bundling.
• This finding offers a method to independently tune fibrin network permeability and elasticity.
• Buffer effects on fibrin assembly may have implications for in vivo clot formation and other biomolecular self-assembly processes.