Modulation of fibrin matrix properties via knob:hole affinity interactions using peptide–PEG conjugates

摘要: Fibrin is a widely used biological scaffold in tissue engineering and regenerative medicine. While the polymerization dynamics from its soluble precursor fibrinogen has been studied for decades, few attempts have made to modulate fibrin network structure through addition of external agents that actively engage this process. We propose use polyethylene glycol (PEG)-based linkers interact with via knob:hole affinity interactions as means controlling thrombin-mediated resulting structure. Using bivalent tetravalent knob-PEG conjugates sizes ranging 2 20 kDa, we demonstrate clotting characteristics solutions can be altered dose-dependent manner, conjugate size playing major role altering Interestingly, factor XIIIa-catalyzed fibrin(ogen) crosslinking plasmin-mediated degradation were not significantly impacted. This work demonstrates feasibility modulating perturb process non-covalent interactions.