ArticleBiochemistry2012
On the mechanism of αC polymer formation in fibrin.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Structural Mechanisms of Forced Unfolding of Double-Stranded Fibrin Oligomers.The journal of physical chemistry. B · 2025Article
- Article
- Systematic mapping of the conformational landscape and dynamism of soluble fibrinogen.Journal of thrombosis and haemostasis : JTH · 2023Article
- Article
- The Story of the Fibrin(ogen) αC-Domains: Evolution of Our View on Their Structure and Interactions.Thrombosis and haemostasis · 2022Review
- Application of optical tweezers in cardiovascular research: More than just a measuring tool.Frontiers in bioengineering and biotechnology · 2022Review
- Strength, deformability and toughness of uncrosslinked fibrin fibers from theoretical reconstruction of stress-strain curves.Acta biomaterialia · 2021Article
- Tracking oxidation-induced alterations in fibrin clot formation by NMR-based methods.Scientific reports · 2021Article
- Missing regions within the molecular architecture of human fibrin clots structurally resolved by XL-MS and integrative structural modeling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Oxidation-induced destabilization of the fibrinogen αC-domain dimer investigated by molecular dynamics simulations.Proteins · 2019Article
- Fibrinogen αC domain: Its importance in physiopathology.Research and practice in thrombosis and haemostasis · 2019Review
- Atomic Structural Models of Fibrin Oligomers.Structure (London, England : 1993) · 2018Article
- Effect of fibrinogen, fibrin, and fibrin degradation products on transendothelial migration of leukocytes.Thrombosis research · 2018Article
- Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization.Nanoscale · 2017Article
- Fibrin mechanical properties and their structural origins.Matrix biology : journal of the International Society for Matrix Biology · 2017Review
- Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- Biophysical Mechanisms Mediating Fibrin Fiber Lysis.BioMed research international · 2017Review
- Nonuniform Internal Structure of Fibrin Fibers: Protein Density and Bond Density Strongly Decrease with Increasing Diameter.BioMed research international · 2017Article
- Fibrin Formation, Structure and Properties.Sub-cellular biochemistry · 2017Review
- Fibrin Networks Support Recurring Mechanical Loads by Adapting their Structure across Multiple Scales.Biophysical journal · 2016Article
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Authors and funding
7 authors.
Funding
Abstract
Our previous studies revealed that the fibrinogen αC-domains undergo conformational changes and adopt a physiologically active conformation upon their self-association into αC polymers in fibrin. In the present study, we analyzed the mechanism of αC polymer formation and tested our hypothesis that self-association of the αC-domains occurs through the interaction between their N-terminal subdomains and may include β-hairpin swapping. Our binding experiments performed by size-exclusion chromatography and optical trap-based force spectroscopy revealed that the αC-domains self-associate exclusively through their N-terminal subdomains, while their C-terminal subdomains were found to interact with the αC-connectors that tether the αC-domains to the bulk of the molecule. This interaction should reinforce the structure of αC polymers and provide the proper orientation of their reactive residues for efficient cross-linking by factor XIIIa. Molecular modeling of self-association of the N-terminal subdomains confirmed that the hypothesized β-hairpin swapping does not impose any steric hindrance. To "freeze" the conformation of the N-terminal subdomain and prevent the hypothesized β-hairpin swapping, we introduced by site-directed mutagenesis an extra disulfide bond between two β-hairpins of the bovine Aα406-483 fragment corresponding to this subdomain. The experiments performed by circular dichroism revealed that Aα406-483 mutant containing Lys429Cys/Thr463Cys mutations preserved its β-sheet structure. However, in contrast to wild-type Aα406-483, this mutant had lower tendency for oligomerization, and its structure was not stabilized upon oligomerization, in agreement with the above hypothesis. On the basis of the results obtained and our previous findings, we propose a model of fibrin αC polymer structure and molecular mechanism of assembly.
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