Structural investigation of PEG-fibrinogen conjugates

Controllable bio-synthetic polymeric hydrogels made from fibrinogen-poly(ethylene glycol) adducts have been successfully employed in tissue engineering. The structural consequences of PEG conjugation to fibrinogen (i.e., PEGylation) in such a hydrogel network are not fully understood. The current investigation details the structural alterations caused to the reduced fibrinogen polypeptides by the covalent attachment of linear or branched PEG chains. The structure of PEGylated fibrinogen polypeptides were comprehensively characterized using small angle X-ray scattering, light scattering, and cryo-transmission electron microscopy. These characterizations concur that the bio-synthetic hybrids self-assemble into elongated objects, having a protein core of about 50 A in diameter decorated with multiple PEG chains. Conjugates with branched PEG chains were shorter, and have lower average molecular weight compared to conjugates with linear chains. The diameter of the protein core of both samples was similar, suggesting a tail-to-head aggregation of the PEGylated fibrinogen polypeptide. A more complete understanding of this unique structural arrangement can provide further insight into the full extent of biofunctional accessibility in a biomaterial that combines the advantages of synthetic polymers with bioactive proteins.