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Thromb Haemost 1997; 77(06): 1048-1051
DOI: 10.1055/s-0038-1656109
Rapid Communications
Schattauer GmbH Stuttgart

Three Dimensional Structure of Human Fibrinogen under Aqueous Conditions Visualized by Atomic Force Microscopy

Roger E Marchant
1   The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
2   Department of Macromolecular Science, Case Western Reserve University, Cleveland Clinic Foundation, Cleveland, Ohio, USA
,
Matthew D Barb
1   The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
,
John R Shainoff
3   The Department of Cell Biology, Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio, USA
,
Steven J Eppell
1   The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
,
David L Wilson
1   The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
,
Christopher A Siedlecki
1   The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
› Author Affiliations
Further Information

Publication History

Received 16 December 1996

Accepted after revision 12 February 1997

Publication Date:
12 July 2018 (online)

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Summary

Fibrinogen plays a central role in surface-induced thrombosis. However, the interactions of fibrinogen with different substrata remain poorly understood because of the difficulties involved in imaging globular proteins under aqueous conditions. We present detailed three dimensional molecular scale images of fibrinogen molecules on a hydrophobic surface under aqueous conditions obtained by atomic force microscopy. Hydrated fibrinogen monomers are visualized as overlapping ellipsoids; dimers and trimers have linear conformations predominantly, and increased affinity for the hydrophobic surface compared with monomeric fibrinogen. The results demonstrate the importance of hydration on protein structure and properties that affect surface-dependent interactions.

 

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