دورية أكاديمية
Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-β using NMR spectroscopy.
| العنوان: | Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-β using NMR spectroscopy. |
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| المؤلفون: | Sun N; ICS-6, Forschungszentrum Jülich, 52425 Jülich, Germany., Hartmann R, Lecher J, Stoldt M, Funke SA, Gremer L, Ludwig HH, Demuth HU, Kleinschmidt M, Willbold D |
| المصدر: | Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2012 Nov; Vol. 18 (11), pp. 691-5. Date of Electronic Publication: 2012 Sep 24. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: John Wiley & Sons Country of Publication: England NLM ID: 9506309 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1099-1387 (Electronic) Linking ISSN: 10752617 NLM ISO Abbreviation: J Pept Sci Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Chichester, West Sussex, UK : John Wiley & Sons, c1995- |
| مواضيع طبية MeSH: | Magnetic Resonance Spectroscopy*, Amyloid beta-Peptides/*chemistry , Pyrrolidonecarboxylic Acid/*chemistry, Alzheimer Disease/pathology ; Humans ; Protein Isoforms/chemistry |
| مستخلص: | The aggregation of the Aβ plays a fundamental role in the pathology of AD. Recently, N-terminally modified Aβ species, pE-Aβ, have been described as major constituents of Aβ deposits in the brains of AD patients. pE-Aβ has an increased aggregation propensity and shows increased toxicity compared with Aβ1-40 and Aβ1-42. In the present work, high-resolution NMR spectroscopy was performed to study pE-Aβ3-40 in aqueous TFE-containing solution. Two-dimensional TOCSY and NOESY experiments were performed. On the basis of NOE and chemical shift data, pE-Aβ3-40 was shown to contain two helical regions formed by residues 14-22 and 30-36. This is similar as previously described for Aβ1-40. However, the secondary chemical shift data indicate decreased helical propensity in pE-Aβ3-40 when compared with Aβ1-40 under exactly the same conditions. This is in agreement with the observation that pE-Aβ3-40 shows a drastically increased tendency to form β-sheet-rich structures under more physiologic conditions. Structural studies of pE-Aβ are crucial for better understanding the structural basis of amyloid fibril formation in the brain during development of AD, especially because an increasing number of reports indicate a decisive role of pE-Aβ for the pathogenesis of AD. (Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.) |
| المشرفين على المادة: | 0 (Amyloid beta-Peptides) 0 (Protein Isoforms) SZB83O1W42 (Pyrrolidonecarboxylic Acid) |
| تواريخ الأحداث: | Date Created: 20120925 Date Completed: 20130419 Latest Revision: 20220317 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1002/psc.2456 |
| PMID: | 23001756 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1099-1387 |
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| DOI: | 10.1002/psc.2456 |