دورية أكاديمية

MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.

التفاصيل البيبلوغرافية
العنوان: MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.
المؤلفون: Manuel Hora, Riddhiman Sarkar, Vanessa Morris, Kai Xue, Elke Prade, Emma Harding, Johannes Buchner, Bernd Reif
المصدر: PLoS ONE, Vol 12, Iss 7, p e0181799 (2017)
بيانات النشر: Public Library of Science (PLoS), 2017.
سنة النشر: 2017
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: Little structural information is available so far on amyloid fibrils consisting of immunoglobulin light chains. It is not understood which features of the primary sequence of the protein result in fibril formation. We report here MAS solid-state NMR studies to identify the structured core of κ-type variable domain light chain fibrils. The core contains residues of the CDR2 and the β-strands D, E, F and G of the native immunoglobulin fold. The assigned core region of the fibril is distinct in comparison to the core identified in a previous solid-state NMR study on AL-09 by Piehl at. al, suggesting that VL fibrils can adopt different topologies. In addition, we investigated a soluble oligomeric intermediate state, previously termed the alternatively folded state (AFS), using NMR and FTIR spectroscopy. The NMR oligomer spectra display a high degree of similarity when compared to the fibril spectra, indicating a high structural similarity of the two aggregation states. Based on comparison to the native state NMR chemical shifts, we suggest that fibril formation via domain-swapping seems unlikely. Moreover, we used our results to test the quality of different amyloid prediction algorithms.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
العلاقة: http://europepmc.org/articles/PMC5528828?pdf=renderTest; https://doaj.org/toc/1932-6203Test
DOI: 10.1371/journal.pone.0181799
الوصول الحر: https://doaj.org/article/8385323faf984c73a88bfdb03891255dTest
رقم الانضمام: edsdoj.8385323faf984c73a88bfdb03891255d
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0181799