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Self-Assembly of Soluble Unlinked and Cross-Linked Fibrin Oligomers

M. A. Rosenfeld*, V. B. Leonova, M. I. Biryukova, and M. V. Vasileva

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, 119334 Moscow, Russia; fax: (495) 137-4101; E-mail: markrosenfeld@rambler.ru

* To whom correspondence should be addressed.

Received February 16, 2011; Revision received June 9, 2011
Self-assembly of soluble unlinked and cross-linked fibrin oligomers formed from desA-fibrin monomer under the influence of factor XIIIa was studied in the presence of non-denaturing urea concentrations. By methods of elastic and dynamic light scattering combined with analytical ultracentrifugation, desA-fibrin oligomers formed in both the presence and absence of the factor XIIIa were shown to be ensembles consisting of soluble rod-like double-stranded protofibrils with diverse weight and size. Unlinked and cross-linked soluble double-stranded protofibrils can reach the length of 350-450 nm. The structure of soluble covalently-linked protofibrils is stabilized by isopeptide γ-dimers. Electrophoretic data indicate a complete absence of isopeptide bonds between α-chains of desA-fibrin molecules. The molecular mechanism of formation of soluble rod-like fibrin structures and specific features of its covalent stabilization under the influence of factor XIIIa are discussed.
KEY WORDS: soluble fibrin, double-stranded protofibrils, factor XIIIa, γ-dimers, α-polymers

DOI: 10.1134/S0006297911100099