دورية أكاديمية
أعرض في EDS

Nanostructure and dynamics of N-truncated copper amyloid-β peptides from advanced X-ray absorption fine structure.

التفاصيل البيبلوغرافية
العنوان: Nanostructure and dynamics of N-truncated copper amyloid-β peptides from advanced X-ray absorption fine structure.
المؤلفون: Ekanayake RSK; School of Physics, University of Melbourne, Australia., Streltsov VA; School of Physics, University of Melbourne, Australia., Best SP; School of Chemistry, University of Melbourne, Australia., Chantler CT; School of Physics, University of Melbourne, Australia.
المصدر: IUCrJ [IUCrJ] 2024 May 01; Vol. 11 (Pt 3), pp. 325-346. Date of Electronic Publication: 2024 May 01.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: International Union of Crystallography Country of Publication: England NLM ID: 101623101 Publication Model: Electronic Cited Medium: Internet ISSN: 2052-2525 (Electronic) Linking ISSN: 20522525 NLM ISO Abbreviation: IUCrJ Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Chester : International Union of Crystallography, [2014]-
مواضيع طبية MeSH: Amyloid beta-Peptides*/metabolism , Amyloid beta-Peptides*/chemistry , Copper*/chemistry , Copper*/metabolism , X-Ray Absorption Spectroscopy*/methods, Humans ; Nanostructures/chemistry ; Binding Sites ; Oxidation-Reduction
مستخلص: An X-ray absorption spectroscopy (XAS) electrochemical cell was used to collect high-quality XAS measurements of N-truncated Cu:amyloid-β (Cu:Aβ) samples under near-physiological conditions. N-truncated Cu:Aβ peptide complexes contribute to oxidative stress and neurotoxicity in Alzheimer's patients' brains. However, the redox properties of copper in different Aβ peptide sequences are inconsistent. Therefore, the geometry of binding sites for the copper binding in Aβ 4-8/12/16 was determined using novel advanced extended X-ray absorption fine structure (EXAFS) analysis. This enables these peptides to perform redox cycles in a manner that might produce toxicity in human brains. Fluorescence XAS measurements were corrected for systematic errors including defective-pixel data, monochromator glitches and dispersion of pixel spectra. Experimental uncertainties at each data point were measured explicitly from the point-wise variance of corrected pixel measurements. The copper-binding environments of Aβ 4-8/12/16 were precisely determined by fitting XAS measurements with propagated experimental uncertainties, advanced analysis and hypothesis testing, providing a mechanism to pursue many similarly complex questions in bioscience. The low-temperature XAS measurements here determine that Cu II is bound to the first amino acids in the high-affinity amino-terminal copper and nickel (ATCUN) binding motif with an oxygen in a tetragonal pyramid geometry in the Aβ 4-8/12/16 peptides. Room-temperature XAS electrochemical-cell measurements observe metal reduction in the Aβ 4-16 peptide. Robust investigations of XAS provide structural details of Cu II binding with a very different bis-His motif and a water oxygen in a quasi-tetrahedral geometry. Oxidized XAS measurements of Aβ 4-12/16 imply that both Cu II and Cu III are accommodated in an ATCUN-like binding site. Hypotheses for these Cu I , Cu II and Cu III geometries were proven and disproven using the novel data and statistical analysis including F tests. Structural parameters were determined with an accuracy some tenfold better than literature claims of past work. A new protocol was also developed using EXAFS data analysis for monitoring radiation damage. This gives a template for advanced analysis of complex biosystems.
(open access.)
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فهرسة مساهمة: Keywords: N-truncated copper amyloid-β peptides; X-ray absorption fine structure; XAS electrochemical cells; binding motifs; nanostructure; radiation damage; redox cycles
المشرفين على المادة: 0 (Amyloid beta-Peptides)
789U1901C5 (Copper)
تواريخ الأحداث: Date Created: 20240411 Date Completed: 20240503 Latest Revision: 20240523
رمز التحديث: 20240523
مُعرف محوري في PubMed: PMC11067746
DOI: 10.1107/S2052252524001830
PMID: 38602752
قاعدة البيانات: MEDLINE
الوصف
تدمد:2052-2525
DOI:10.1107/S2052252524001830