دورية أكاديمية
Aggregation-Prone Amyloid-β⋅Cu(II) Species Formed on the Millisecond Timescale under Mildly Acidic Conditions.
| العنوان: | Aggregation-Prone Amyloid-β⋅Cu(II) Species Formed on the Millisecond Timescale under Mildly Acidic Conditions. |
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| المؤلفون: | Pedersen JT; Department of Pharmaceutics, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen (Denmark). jeppe.trudslev@sund.ku.dk., Borg CB; Department of Biology, University of Copenhagen, Ole Maaløesvej 5, 2200 Copenhagen (Denmark)., Michaels TC; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW (UK)., Knowles TP; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW (UK)., Faller P; Université de Toulouse; UPS, INPT 31077 Toulouse (France) and LCC (Laboratoire de Chimie de Coordination), CNRS UPR 8241 205, Route de Narbonne, 31077 Toulouse Cedex 4 (France)., Teilum K; Department of Biology, University of Copenhagen, Ole Maaløesvej 5, 2200 Copenhagen (Denmark)., Hemmingsen L; Department of Chemistry, University of Copenhagen, Universitetsparken 5, 2100 Copenhagen (Denmark). lhe@chem.ku.dk. |
| المصدر: | Chembiochem : a European journal of chemical biology [Chembiochem] 2015 Jun 15; Vol. 16 (9), pp. 1293-7. Date of Electronic Publication: 2015 May 18. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Wiley-VCH Verlag Country of Publication: Germany NLM ID: 100937360 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1439-7633 (Electronic) Linking ISSN: 14394227 NLM ISO Abbreviation: Chembiochem Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Weinheim, Germany : Wiley-VCH Verlag, c2000- |
| مواضيع طبية MeSH: | Amyloid beta-Peptides/*metabolism , Copper/*metabolism, Acidosis/metabolism ; Alzheimer Disease/metabolism ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Nuclear Magnetic Resonance, Biomolecular ; Protein Aggregates ; Protein Aggregation, Pathological/metabolism |
| مستخلص: | Metal ions and their interaction with the amyloid beta (Aβ) peptide might be key elements in the development of Alzheimer's disease. In this work the effect of Cu(II) on the aggregation of Aβ is explored on a timescale from milliseconds to days, both at physiological pH and under mildly acidic conditions, by using stopped-flow kinetic measurements (fluorescence and light-scattering), (1) H NMR relaxation and ThT fluorescence. A minimal reaction model that relates the initial Cu(II) binding and Aβ folding with downstream aggregation is presented. We demonstrate that a highly aggregation prone Aβ⋅Cu(II) species is formed on the sub-second timescale at mildly acidic pH. This observation might be central to the molecular origin of the known detrimental effect of acidosis in Alzheimer's disease. (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.) |
| فهرسة مساهمة: | Keywords: NMR spectroscopy; amyloid beta-peptides; copper; kinetics; stopped-flow |
| المشرفين على المادة: | 0 (Amyloid beta-Peptides) 0 (Protein Aggregates) 789U1901C5 (Copper) |
| تواريخ الأحداث: | Date Created: 20150520 Date Completed: 20160301 Latest Revision: 20150606 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1002/cbic.201500080 |
| PMID: | 25989377 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1439-7633 |
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| DOI: | 10.1002/cbic.201500080 |