Transmission electron microscopy study of co-polymers of fibrinogen with N-terminal disulfide knot of fibrin

The structure of co-polymers of fibrinogen (F) with N-terminal disulfide knot of desAABB fibrin (tN-DSK) was investigated by transmission electron microscopy of their negatively contrasted samples. It was shown that the co-polymers initial forms were represented by short threads of 2–4 end-to-end ar...

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Published inBiopolimery i kletka Vol. 13; no. 4; pp. 291 - 297
Main Authors Pozdnjakova, T. M., Chernishov, V. I., Makogonenko, E. M., Chernishenko, T. M., Cederholm-Williams, S. A.
Format Journal Article
LanguageEnglish
Published Kiev Natsional'na Akademiya Nauk Ukrainy - National Academy of Sciences of Ukraine 1997
Subjects
Copolymers
Fibrillogenesis
Fibrin
Fibrinogen
Polymerization
Polymers
Self-assembly
Thrombin
Transmission electron microscopy
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Summary:The structure of co-polymers of fibrinogen (F) with N-terminal disulfide knot of desAABB fibrin (tN-DSK) was investigated by transmission electron microscopy of their negatively contrasted samples. It was shown that the co-polymers initial forms were represented by short threads of 2–4 end-to-end arranged F molecules, in which tN-DSK molecules could't be visualized by the used method. Then long single-threaded structures formed which aggregated laterally in fibril-like bunches of varying thickness. The network of fibrils have arisen finally. In control experiments when in the fibrinogen containing samples tN-DSK was substituted for thrombin, one could observe the double-threaded twisted protofibrils but not any of the single-threaded end-to-end arranged molecules. These studies confirm the hypothetical model of F-tN-DSK co-polymer structure as the thread of end-to-end arranged fibrinogen molecules, the adjacent D-domain of which are bound by tN-DSK molecules via the fibrin polymerization sites. The lateral aggregation of co-polymer strains into fibrils and fibril network formation revealed in this study is the evidence of similarity between F-tN-DSK co-polymers and. fibrin polymer structures. It is not wonder because both structures are formed by the unique self-assembly mechanism in which the noncovalent binding of fibrin(ogen) molecules by the complementary fibrin polymerization sites is involved.
ISSN:0233-7657
1993-6842
DOI:10.7124/bc.00048D