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大学・研究所にある論文を検索できる 「A novel variant fibrinogen, AαE11del, demonstrating the importance of AαE11 residue in thrombin binding」の論文概要。リケラボ論文検索は、全国の大学リポジトリにある学位論文・教授論文を一括検索できる論文検索サービスです。
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A novel variant fibrinogen, AαE11del, demonstrating the importance of AαE11 residue in thrombin binding

Kaido, Takahiro Yoda, Masahiro Kamijo, Tomu Arai, Shinpei Yamauchi, Kazuyoshi Okumura, Nobuo 信州大学 DOI:34333754

2022.01.04

概要

Introduction: We identified a novel heterozygous AαE11del variant in a patient with congenital dysfibrinogenemia. This mutation is located in fibrinopeptide A (FpA). We analyzed the effect of AαE11del on the catalyzation of thrombin and batroxobin and simulated the stability of the complex structure between the FpA fragment (AαG6-V20) peptide and thrombin.

Materials and Methods: We performed fibrin polymerization and examined the kinetics of FpA release catalyzed by thrombin and batroxobin using purified plasma fibrinogen. To clarify the association between the AαE11 residue and thrombin, we calculated binding free energy using molecular dynamics simulation trajectories.

Results: Increasing the thrombin concentration improved release of FpA from the patient’s fibrinogen to approximately 90%, compared to the previous 50% of that of normal fibrinogen. Fibrin polymerization of variant fibrinogen also improved. In addition, greater impairment of variant FpA release from the patient’s fibrinogen was observed with thrombin than with batroxobin. Moreover, the calculated binding free energy showed that the FpA fragment– thrombin complex became unstable due to the missing AαE11 residue.

Conclusions: Our findings indicate that the AαE11 residue is involved in FpA release in thrombin catalyzation more than in batroxobin catalyzation, and that the AαE11 residue stabilizes FpA fragment–thrombin complex formation.

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