کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5370717 1503902 2016 13 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Regulation of the assembly and amyloid aggregation of murine amylin by zinc
ترجمه فارسی عنوان
تنظیم مونتاژ و تجمع آمیلوئید آمیلین موش توسط روی
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
چکیده انگلیسی


- Zinc interacts with murine amylin as measured by zincon, SPR, fluorescence, IMS, NMR.
- Zinc is a heterotrophic modulator of murine amylin assembly and aggregation.
- Zinc regulation of amylin does not require the His residue.

The secretory granule of the pancreatic β-cells is a zinc-rich environment copopulated with the hormones amylin and insulin. The human amylin is shown to interact with zinc ions with major contribution from the single histidine residue, which is absent in amylin from other species such as cat, rhesus and rodents. We report here the interaction of murine amylin with zinc ions in vitro. The self-assembly of murine amylin is tightly regulated by zinc and pH. Ion mobility mass spectrometry revealed zinc interaction with monomers and oligomers. Nuclear magnetic resonance confirms the binding of zinc to murine amylin. The aggregation process of murine amylin into amyloid fibrils is accelerated by zinc. Collectively these data suggest a general role of zinc in the modulation of amylin variants oligomerization and amyloid fibril formation.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 218, November 2016, Pages 58-70
نویسندگان
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