دورية أكاديمية
Molecular basis of a redox switch: molecular dynamics simulations and surface plasmon resonance provide insight into reduced and oxidised angiotensinogen.
| العنوان: | Molecular basis of a redox switch: molecular dynamics simulations and surface plasmon resonance provide insight into reduced and oxidised angiotensinogen. |
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| المؤلفون: | Crowther JM; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.; School of Biological Sciences, University of Canterbury, Christchurch, New Zealand., Gilmour LH; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.; School of Biological Sciences, University of Canterbury, Christchurch, New Zealand., Porebski BT; Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia.; Medical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge, U.K., Heath SG; Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch, New Zealand., Pattinson NR; Canterbury Scientific, Christchurch, New Zealand., Owen MC; Canterbury Scientific, Christchurch, New Zealand., Fredericks R; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.; Department of Chemical and Process Engineering, University of Canterbury, Christchurch, New Zealand., Buckle AM; Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia., Fee CJ; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.; Department of Chemical and Process Engineering, University of Canterbury, Christchurch, New Zealand.; School of Product Design, University of Canterbury, Christchurch, New Zealand., Göbl C; Centre for Free Radical Research, Department of Pathology, University of Otago, Christchurch, New Zealand., Dobson RCJ; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.; School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria, Australia.; Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand. |
| المصدر: | The Biochemical journal [Biochem J] 2021 Sep 17; Vol. 478 (17), pp. 3319-3330. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R Publication Model: Print Cited Medium: Internet ISSN: 1470-8728 (Electronic) Linking ISSN: 02646021 NLM ISO Abbreviation: Biochem J Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: London, UK : Published by Portland Press on behalf of the Biochemical Society |
| مواضيع طبية MeSH: | Molecular Dynamics Simulation*, Angiotensinogen/*chemistry , Angiotensinogen/*metabolism , Surface Plasmon Resonance/*methods, Angiotensinogen/genetics ; Angiotensinogen/immunology ; Antibodies, Monoclonal/immunology ; Blood Pressure/physiology ; Cysteine/metabolism ; Disulfides/metabolism ; Epitopes/immunology ; Humans ; Kinetics ; Oxidation-Reduction ; Protein Binding ; Protein Conformation, alpha-Helical ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Renin-Angiotensin System/physiology |
| مستخلص: | Angiotensinogen fine-tunes the tightly controlled activity of the renin-angiotensin system by modulating the release of angiotensin peptides that control blood pressure. One mechanism by which this modulation is achieved is via angiotensinogen's Cys18-Cys138 disulfide bond that acts as a redox switch. Molecular dynamics simulations of each redox state of angiotensinogen reveal subtle dynamic differences between the reduced and oxidised forms, particularly at the N-terminus. Surface plasmon resonance data demonstrate that the two redox forms of angiotensinogen display different binding kinetics to an immobilised anti-angiotensinogen monoclonal antibody. Mass spectrometry mapped the epitope for the antibody to the N-terminal region of angiotensinogen. We therefore provide evidence that the different redox forms of angiotensinogen can be detected by an antibody-based detection method. (© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.) |
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| معلومات مُعتمدة: | MC_U105178804 United Kingdom MRC_ Medical Research Council |
| فهرسة مساهمة: | Keywords: angiotensinogen; hypertension; redox-switch |
| المشرفين على المادة: | 0 (AGT protein, human) 0 (Antibodies, Monoclonal) 0 (Disulfides) 0 (Epitopes) 0 (Recombinant Proteins) 11002-13-4 (Angiotensinogen) K848JZ4886 (Cysteine) |
| تواريخ الأحداث: | Date Created: 20210823 Date Completed: 20211203 Latest Revision: 20211218 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC7612104 |
| DOI: | 10.1042/BCJ20210476 |
| PMID: | 34424335 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1470-8728 |
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| DOI: | 10.1042/BCJ20210476 |