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Transport of probe molecules through fibrin gels as observed by means of holographic relaxation methods

Holographic relaxation spectroscopy (HRS) has been used to study transport of benzospiropyran (SP), BSA labeled with azobenzene (BSA‐ABITC), and IgG‐κ labeled with fluorescein (IgG‐FITC) through fibrin gels formed under various conditions. The structures of the gels were controlled by means of the concentrations of fibrinogen, thrombin, and Ca2+ present during assembly of the fibrin. The diffusion coefficient of free dye (SP) was found to be independent of the fibrinogen concentration. The diffusion rate of labeled BSA reflected the assembly conditions of the gel for fibrinogen concentrations above approximately 6 g/L. In particular, the diffusion coefficient was higher in gels formed in the presence of 5 mM Ca2+. The labeled IgG showed photoinduced aggregation, as previously reported, as well as photoinduced attachment to the gel network to produce a permanent diffraction grating. Thus IgG is not a probe in the classical sense, but provides a model for protein diffusion and interactions in gels. These studies indicate that HRS is well suited to the study of molecular transport in fibrin gels.