کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5371096 1503933 2013 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Stepwise oligomerization of murine amylin and assembly of amyloid fibrils
ترجمه فارسی عنوان
الیگومریزاسیون گامی آمیلیون قارچ و مونتاژ فیبریل آمیلوئید
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
چکیده انگلیسی


- Murine amylin spontaneously associate in low and high order oligomers.
- Murine amylin forms aggregates with amyloid fibril morphology.
- Proline-rich amylin is also capable to form amyloid structures in vitro.

Amylin is a pancreatic hormone co-secreted with insulin. Human amylin has been shown to form dimers and exhibit high propensity for amyloid fibril formation. We observed the ability of the water-soluble murine amylin to aggregate in water resulting in an insoluble material with Thioflavin T binding properties. Infrared spectroscopy analysis revealed beta-sheet components in the aggregated murine amylin. Morphological analysis by transmission electron microscopy and atomic force microscopy provided access to the fibril nature of the murine amylin aggregate which is similar to amyloid fibrils from human amylin. X-ray diffraction of the murine amylin fibrils showed peaks at 4.7 Å and 10 Å, a fingerprint for amyloid fibrils. Electron spray ionization-ion mobility spectroscopy-mass spectrometry (ESI-IMS-MS) analysis and crosslinking assays revealed self-association intermediates of murine amylin into high order oligomeric assemblies. These data demonstrate the stepwise association mechanism of murine amylin into stable oligomers, which ultimately converges to its organization into amyloid fibrils.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volumes 180–181, October–November 2013, Pages 135-144
نویسندگان
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