ArticleBiochemistry2009
Structure, stability, and interaction of the fibrin(ogen) alphaC-domains.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- 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
- Engineered Molecular Therapeutics Targeting Fibrin and the Coagulation System: a Biophysical Perspective.Biophysical reviews · 2022Review
- Article
- Anomalous mechanics of ZnProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Fibrinogen αC-regions are not directly involved in fibrin polymerization as evidenced by a "Double-Detroit" recombinant fibrinogen mutant and knobs-mimic peptides.Journal of thrombosis and haemostasis : JTH · 2020Article
- Adsorption of Fibrinogen on Silica Surfaces-The Effect of Attached Nanoparticles.Biomolecules · 2020Article
- Oxidation-induced destabilization of the fibrinogen αC-domain dimer investigated by molecular dynamics simulations.Proteins · 2019Article
- Atomic Structural Models of Fibrin Oligomers.Structure (London, England : 1993) · 2018Article
- Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry.Doklady. Biochemistry and biophysics · 2018Article
- 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 Fiber Stiffness Is Strongly Affected by Fiber Diameter, but Not by Fibrinogen Glycation.Biophysical journal · 2016Article
- Article
- Polymerisation of fibrin αC-domains promotes endothelial cell migration and proliferation.Thrombosis and haemostasis · 2014Article
- Structural effects of methionine oxidation on isolated subdomains of human fibrin D and αC regions.PloS one · 2014Article
- Fibrinogen species as resolved by HPLC-SAXS data processing within theJournal of applied crystallography · 2013Article
- Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry.Biochemistry · 2013Article
- Hydrodynamic characterization of recombinant human fibrinogen species.Thrombosis research · 2013Article
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Authors and funding
6 authors.
Funding
Abstract
Our recent study established the NMR structure of the recombinant bAalpha406-483 fragment corresponding to the NH(2)-terminal half of the bovine fibrinogen alphaC-domain and revealed that at increasing concentrations this fragment forms oligomers (self-associates). The major goals of the study presented here were to determine the structure and self-association of the full-length human fibrinogen alphaC-domains. To accomplish these goals, we prepared a recombinant human fragment, hAalpha425-503, homologous to bovine bAalpha406-483, and demonstrated using NMR, CD, and size-exclusion chromatography that its overall fold and ability to form oligomers are similar to those of bAalpha406-483. We also prepared recombinant hAalpha392-610 and bAalpha374-568 fragments corresponding to the full-length human and bovine alphaC-domains, respectively, and tested their structure, stability, and ability to self-associate. Size-exclusion chromatography revealed that both fragments form reversible oligomers in a concentration-dependent manner. Their oligomerization was confirmed in sedimentation equilibrium experiments, which also established the self-association affinities of these fragments and revealed that the addition of each monomer to assembling alphaC-oligomers substantially increases the stabilizing free energy. In agreement, unfolding experiments monitored by CD established that self-association of both fragments results in a significant increase in their thermal stability. Analysis of CD spectra of both fragments revealed that alphaC self-association results in an increase in the level of regular structure, implying that the COOH-terminal half of the alphaC-domain adopts an ordered conformation in alphaC-oligomers and that this domain contains two independently folded subdomains. Altogether, these data further clarify the structure of the human and bovine alphaC-domains and the molecular mechanism of their self-association into alphaC-polymers in fibrin.
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