Fibrinogenis observed as three bands: α (68 kDa), β (56 kDa), and γ (48 kDa) chains. Bands below 48 kDareflect fibrinogen cleavage by thrombin . It plays a critical role in the process of blood clotting and serves as a substrate for three interconnected enzymes: plasmin, thrombin, and factor XIIIa . Even the presence of 5 ng/cm 2 of adsorbed fibrinogen has been shown to trigger platelet activation . Comparable to the elastin-like polypeptide nanoparticles investigated earlier , fibrinogen exhibited a strong attachment to PCL membranes with exceptionally high-intensity readings. In this case, UTX presence didn't seem to influence the adsorption of this protein. This was likely due to the overbearing role of the surface area in this adsorption of fibrinogen. However, a low intensity band for the cleavage fragment was detected and decreased in the presence of UTXs. There is now substantial evidence showing that UTXs can directly impact enzymatic function , which may explain this decrease in fibrinogen cleavage when UTXs are present.