[Molecular organization of copolymers of fibrinogen-fibrin fragment].
In this study we have produced for the first time a native fibrinogen copolymer with a fragment of fibrin E. and the molecular mechanism of its formation was studied by different physicochemical methods. Based on the data of angular dependency of the Debay scattering factor, the average molecular mass, coefficients of translational diffusion and the intrinsic viscosity it was shown that the primary interaction comprised the "end-to-end" fibrinogen dimerization through the D-D contacts with the following fragment E specific binding. It resulted in the stable three-domain D-E-D knot formation. The structural flexibility of the copolymer determines the tendency to their folding and the strong intermolecular hydrodynamic interaction indicates the structural compactization. This correlates as we think, with the presence of the centers of lateral binding in the fibrinogen molecule. Single-strand copolymers aggregate when they reach their critical sweep length resulting in microgel formation with the raise of the molecular mass. We came to the conclusion that fibrinogen molecules are capable to associate due to the stable native conformation shift into the active state, thus demasking the reaction groups in the D-domain. Possible reasons for the lack of fibrinogen heteropolymer rigidity characteristic for the fibrin polymers are discussed.
Rozenfel'd
M A
MA
Gershkovich
K B
KB
D000818:Animals; D002417:Cattle; D005338:Fibrin Fibrinogen Degradation Products; D005340:Fibrinogen; D008433:Mathematics; D008958:Models, Molecular; D011108:Polymers; D011487:Protein Conformation
D005338:Fibrin Fibrinogen Degradation Products; D011108:Polymers; C046679:fibrinopeptide E; D005340:Fibrinogen
Molekuliarnaia organizatsiia sopolimerov fibrinogen-fragment fibrina.