دورية أكاديمية

Influence of C-terminal truncation of murine Serum amyloid A on fibril structure

التفاصيل البيبلوغرافية
العنوان: Influence of C-terminal truncation of murine Serum amyloid A on fibril structure
المؤلفون: Matthies Rennegarbe, Inga Lenter, Angelika Schierhorn, Romy Sawilla, Christian Haupt
المصدر: Scientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
بيانات النشر: Nature Portfolio, 2017.
سنة النشر: 2017
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: Abstract Amyloid A (AA) amyloidosis is a systemic protein misfolding disease affecting humans and other vertebrates. While the protein precursor in humans and mice is the acute-phase reactant serum amyloid A (SAA) 1.1, the deposited fibrils consist mainly of C-terminally truncated SAA fragments, termed AA proteins. For yet unknown reasons, phenotypic variations in the AA amyloid distribution pattern are clearly associated with specific AA proteins. Here we describe a bacterial expression system and chromatographic strategies to obtain significant amounts of C-terminally truncated fragments of murine SAA1.1 that correspond in truncation position to relevant pathological AA proteins found in humans. This enables us to investigate systematically structural features of derived fibrils. All fragments form fibrils under nearly physiological conditions that show similar morphological appearance and amyloid-like properties as evident from amyloid-specific dye binding, transmission electron microscopy and infrared spectroscopy. However, infrared spectroscopy suggests variations in the structural organization of the amyloid fibrils that might be derived from a modulating role of the C-terminus for the fibril structure. These results provide insights, which can help to get a better understanding of the molecular mechanisms underlying the different clinical phenotypes of AA amyloidosis.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2045-2322
العلاقة: https://doaj.org/toc/2045-2322Test
DOI: 10.1038/s41598-017-06419-1
الوصول الحر: https://doaj.org/article/b27108d49c674c0499766e0c7a5184f5Test
رقم الانضمام: edsdoj.b27108d49c674c0499766e0c7a5184f5
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20452322
DOI:10.1038/s41598-017-06419-1