Conformational Flexibility and Self-Association of Fibrinogen in Concentrated Solutions
| Autor: | Dennis K. Galanakis, Artem Zhmurov, B. Z. Idiyatullin, Yuriy F. Zuev, Valeri Barsegov, John W. Weisel, Rustem I. Litvinov, Dilyafruz R. Bakirova, Alexander E. Sitnitsky |
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| Rok vydání: | 2017 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation Diffusion Activation energy Fibrinogen Fibrin 03 medical and health sciences symbols.namesake Blood plasma Materials Chemistry medicine Humans Physical and Theoretical Chemistry Pliability Arrhenius equation 030102 biochemistry & molecular biology biology Chemistry GPRP Surfaces Coatings and Films Solutions Crystallography 030104 developmental biology Polymerization Hydrodynamics biology.protein symbols medicine.drug |
| Zdroj: | The Journal of Physical Chemistry B. 121:7833-7843 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.7b05654 |
| Popis: | We studied the hydrodynamic behavior of fibrinogen, a blood plasma protein involved in blood clotting, in a broad 0.3–60 mg/mL range of concentration and 5–42 °C temperature using pulsed-field gradient 1H NMR-diffusometry. Arrhenius plots revealed the activation energy for fibrinogen diffusion Ed = 21.3 kJ/mol at 1.4 mg/mL and 28.4 kJ/mol at 38 mg/mL. We found a dramatic slowdown in fibrinogen self-diffusion with concentration beginning at 1.7–3.4 mg/mL, which deviated from the standard hard-particle behavior, suggesting a remarkable intermolecular entanglement. This concentration dependence was observed regardless of the absence or presence of the GPRP peptide (inhibitor of fibrin polymerization), and also in samples free of fibrin oligomers. By contrast, diffusivity of fibrinogen variant I-9 with truncated C-terminal portions of the Aα chains was much less concentration-dependent, indicating the importance of intermolecular linkages formed by the αC regions. Theoretical models combined with all-atom mol... |
| Databáze: | OpenAIRE |
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